Identification of Chaperones in Freeze Tolerance in Saccharomyces cerevisiae
Exposure to low temperatures reduces protein folding rates and induces the cold denaturation of proteins. Considering the roles played by chaperones in facilitating protein folding and preventing protein aggregation, chaperones must exist that confer tolerance to cold stress. Here, yeast strains lac...
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| Published in | The journal of microbiology Vol. 50; no. 5; pp. 882 - 887 |
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| Main Authors | , , |
| Format | Journal Article |
| Language | English |
| Published |
Heidelberg
The Microbiological Society of Korea
01.10.2012
Springer Nature B.V 한국미생물학회 |
| Subjects | |
| Online Access | Get full text |
| ISSN | 1225-8873 1976-3794 1976-3794 |
| DOI | 10.1007/s12275-012-2411-z |
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| Abstract | Exposure to low temperatures reduces protein folding rates and induces the cold denaturation of proteins. Considering the roles played by chaperones in facilitating protein folding and preventing protein aggregation, chaperones must exist that confer tolerance to cold stress. Here, yeast strains lacking individual chaperones were screened for reduced freezing tolerance. In total, 19 of 82 chaperone-deleted strains tested were more sensitive to freeze-thaw treatment than wild-type cells. The reintroduction of the respective chaperone genes into the deletion mutants recovered the freeze tolerance. The freeze sensitivity of the chaperone-knockout strains was also retained in the presence of 20% glycerol. |
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| AbstractList | Exposure to low temperatures reduces protein folding rates and induces the cold denaturation of proteins. Considering the roles played by chaperones in facilitating protein folding and preventing protein aggregation, chaperones must exist that confer tolerance to cold stress. Here, yeast strains lacking individual chaperones were screened for reduced freezing tolerance. In total, 19 of 82 chaperone-deleted strains tested were more sensitive to freeze-thaw treatment than wild-type cells. The reintroduction of the respective chaperone genes into the deletion mutants recovered the freeze tolerance. The freeze sensitivity of the chaperone-knockout strains was also retained in the presence of 20% glycerol.[PUBLICATION ABSTRACT] Exposure to low temperatures reduces protein folding rates and induces the cold denaturation of proteins. Considering the roles played by chaperones in facilitating protein folding and preventing protein aggregation, chaperones must exist that confer tolerance to cold stress. Here, yeast strains lacking individual chaperones were screened for reduced freezing tolerance. In total, 19 of 82 chaperone-deleted strains tested were more sensitive to freeze-thaw treatment than wild-type cells. The reintroduction of the respective chaperone genes into the deletion mutants recovered the freeze tolerance. The freeze sensitivity of the chaperone-knockout strains was also retained in the presence of 20% glycerol. Exposure to low temperatures reduces protein folding rates and induces the cold denaturation of proteins. Considering the roles played by chaperones in facilitating protein folding and preventing protein aggregation, chaperones must exist that confer tolerance to cold stress. Here, yeast strains lacking individual chaperones were screened for reduced freezing tolerance. In total, 19 of 82 chaperone-deleted strains tested were more sensitive to freeze-thaw treatment than wild-type cells. The reintroduction of the respective chaperone genes into the deletion mutants recovered the freeze tolerance. The freeze sensitivity of the chaperone-knockout strains was also retained in the presence of 20% glycerol.Exposure to low temperatures reduces protein folding rates and induces the cold denaturation of proteins. Considering the roles played by chaperones in facilitating protein folding and preventing protein aggregation, chaperones must exist that confer tolerance to cold stress. Here, yeast strains lacking individual chaperones were screened for reduced freezing tolerance. In total, 19 of 82 chaperone-deleted strains tested were more sensitive to freeze-thaw treatment than wild-type cells. The reintroduction of the respective chaperone genes into the deletion mutants recovered the freeze tolerance. The freeze sensitivity of the chaperone-knockout strains was also retained in the presence of 20% glycerol. Exposure to low temperatures reduces protein folding rates and induces the cold denaturation of proteins. Considering the roles played by chaperones in facilitating protein folding and preventing protein aggregation, chaperones must exist that confer tolerance to cold stress. Here, yeast strains lacking individual chaperones were screened for reduced freezing tolerance. In total, 19 of 82 chaperone-deleted strains tested were more sensitive to freeze-thaw treatment than wild-type cells. The reintroduction of the respective chaperone genes into the deletion mutants recovered the freeze tolerance. The freeze sensitivity of the chaperone-knockout strains was also retained in the presence of 20% glycerol. KCI Citation Count: 7 |
| Author | Im, H.N., Sejong University, Seoul, Republic of Korea Naicker, Mahendran Chinnamara, Sejong University, Seoul, Republic of Korea Jo, I.S., Sejong University, Seoul, Republic of Korea |
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| CitedBy_id | crossref_primary_10_1002_bkcs_11581 crossref_primary_10_3390_fermentation10060318 crossref_primary_10_1152_physrev_00016_2016 crossref_primary_10_3390_ijms26052149 crossref_primary_10_1091_mbc_E22_07_0262 crossref_primary_10_1007_s00018_018_2821_0 crossref_primary_10_1002_bkcs_10685 crossref_primary_10_1002_bkcs_12289 |
| Cites_doi | 10.1016/S1097-2765(04)00148-0 10.3109/10409239009090612 10.1038/nature00935 10.4161/pri.3.2.8587 10.1073/pnas.94.10.4978 10.1083/jcb.143.4.921 10.1074/jbc.275.8.5767 10.1073/pnas.87.13.4986 10.1073/pnas.94.24.12949 10.1007/BF00340712 10.1073/pnas.121172998 10.1083/jcb.150.1.65 10.1083/jcb.129.4.979 10.1093/emboj/19.11.2444 10.1093/nar/gki126 10.1073/pnas.94.24.13093 10.1038/sj.embor.7400662 10.1093/emboj/19.7.1486 10.1016/S0092-8674(00)80928-9 10.1091/mbc.E04-09-0807 10.1534/genetics.112.140319 10.1007/s00294-008-0193-y 10.1073/pnas.90.12.5450 10.1073/pnas.92.14.6319 10.1007/s10059-010-0071-6 10.1016/0076-6879(91)94030-G 10.1074/jbc.274.38.26654 10.1073/pnas.132275199 10.1007/s12192-010-0215-9 10.1534/genetics.108.089458 10.1128/jb.169.5.2092-2095.1987 10.1128/MCB.18.12.7353 10.1128/MCB.7.7.2568 |
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| Keywords | cold shock response chaperone yeast freeze tolerance |
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| References | Douglas, Summers, Cyr (CR7) 2009; 3 Partaledis, Berlin (CR21) 1993; 90 Kandror, Bretschneider, Kreydin, Cavalieri, Goldberg (CR11) 2004; 13 Silberstein, Schlenstedt, Silver, Gilmore (CR30) 1998; 143 Ackerman, Tzagoloff (CR1) 1990; 87 Nijtmans, de -Jong, Sanz, Coates, Berden, Back, Muijsers, Van der -Speck, Grivell (CR20) 2000; 19 Tatsuta, Model, Langer (CR31) 2005; 16 Jones, VanBogelen, Neidhardt (CR10) 1987; 169 Kim, Kim, Shin, Kim, Lee, Park, Yoon (CR14) 2010; 29 Privalov (CR23) 1990; 25 Seki, Kleinhans, Mazur (CR26) 2009; 58 Marsh, Kalton, Gaber (CR17) 1998; 18 Matouschek, Rospert, Schmid, Glick, Schatz (CR18) 1995; 92 Werner-Washburne, Stone, Craig (CR35) 1987; 7 Birrell, Brown, Wu, Giaever, Chu, Davis, Brown (CR2) 2002; 99 Liu, Morano, Thiele (CR16) 1999; 274 Sharma, Masison (CR29) 2011; 33 Phadtare (CR22) 2004; 6 Schlenstedt, Harris, Risse, Lill, Silver (CR25) 1995; 129 Trotter, Berenfeld, Krause, Petsko, Gray (CR32) 2001; 98 Zuehlke, Johnson (CR36) 2012; 191 Wang, Sheluho, Gatti, Ackerman (CR34) 2000; 19 Nathan, Harju-Vos, Lindquist (CR19) 1997; 94 Kandror, Goldberg (CR12) 1997; 94 Kohrer, Domdey (CR15) 1991; 194 Shaner, Gibney, Morano (CR27) 2008; 54 Dolinski, Muir, Cardenas, Heitman (CR6) 1997; 94 Schiestl, Gietz (CR24) 1989; 16 Brown, McCann, Chiang (CR3) 2000; 150 D’Amico, Collins, Marx, Feller, Gerday (CR5) 2006; 7 Bukau, Horwich (CR4) 1998; 92 Wang, Ackerman (CR33) 2000; 275 Kim, Jin, Yoon (CR13) 2011; 16 Fernandez-Ricaud, Warringer, Ericson, Pylvanainen, Kemp, Nerman, Blomberg (CR8) 2005; 33 Sharma, Masison (CR28) 2008; 179 Giaever, Chu, Ni, Connelly, Riles, Véronneau, Dow, Lucau-Danila, Anderson, André (CR9) 2002; 418 L. Shaner (2411_CR27) 2008; 54 O. Kandror (2411_CR12) 1997; 94 P.L. Privalov (2411_CR23) 1990; 25 R.H. Schiestl (2411_CR24) 1989; 16 J.A. Marsh (2411_CR17) 1998; 18 S. Phadtare (2411_CR22) 2004; 6 T. Tatsuta (2411_CR31) 2005; 16 G.W. Birrell (2411_CR2) 2002; 99 J.A. Partaledis (2411_CR21) 1993; 90 G. Schlenstedt (2411_CR25) 1995; 129 S.H. Ackerman (2411_CR1) 1990; 87 C.R. Brown (2411_CR3) 2000; 150 L. Fernandez-Ricaud (2411_CR8) 2005; 33 B. Bukau (2411_CR4) 1998; 92 Z.G. Wang (2411_CR33) 2000; 275 K. Dolinski (2411_CR6) 1997; 94 P.M. Douglas (2411_CR7) 2009; 3 D.F. Nathan (2411_CR19) 1997; 94 G. Giaever (2411_CR9) 2002; 418 A. Matouschek (2411_CR18) 1995; 92 S. Silberstein (2411_CR30) 1998; 143 P.G. Jones (2411_CR10) 1987; 169 O. Kandror (2411_CR11) 2004; 13 I.S. Kim (2411_CR13) 2011; 16 L.G.J. Nijtmans (2411_CR20) 2000; 19 E.W. Trotter (2411_CR32) 2001; 98 S. Seki (2411_CR26) 2009; 58 S. D’Amico (2411_CR5) 2006; 7 K. Kohrer (2411_CR15) 1991; 194 D. Sharma (2411_CR28) 2008; 179 D. Sharma (2411_CR29) 2011; 33 A.D. Zuehlke (2411_CR36) 2012; 191 X.D. Liu (2411_CR16) 1999; 274 I.S. Kim (2411_CR14) 2010; 29 Z.G. Wang (2411_CR34) 2000; 19 M. Werner-Washburne (2411_CR35) 1987; 7 9144175 - Proc Natl Acad Sci U S A. 1997 May 13;94(10):4978-81 9371781 - Proc Natl Acad Sci U S A. 1997 Nov 25;94(24):12949-56 11416208 - Proc Natl Acad Sci U S A. 2001 Jun 19;98 (13):7313-8 9819422 - Mol Cell Biol. 1998 Dec;18(12):7353-9 2142305 - Proc Natl Acad Sci U S A. 1990 Jul;87(13):4986-90 3553157 - J Bacteriol. 1987 May;169(5):2092-5 12077312 - Proc Natl Acad Sci U S A. 2002 Jun 25;99(13):8778-83 19118541 - Cryobiology. 2009 Apr;58(2):157-65 15608218 - Nucleic Acids Res. 2005 Jan 1;33(Database issue):D369-73 9817751 - J Cell Biol. 1998 Nov 16;143(4):921-33 20680535 - Cell Stress Chaperones. 2011 Jan;16(1):1-14 16585939 - EMBO Rep. 2006 Apr;7(4):385-9 7685904 - Proc Natl Acad Sci U S A. 1993 Jun 15;90(12):5450-4 22505624 - Genetics. 2012 Jul;191(3):805-14 20496120 - Mol Cells. 2010 Jun;29(6):567-74 18478233 - Curr Genet. 2008 Jul;54(1):1-11 21808014 - Proc Natl Acad Sci U S A. 2011 Aug 16;108(33):13665-70 19421006 - Prion. 2009 Apr-Jun;3(2):51-8 10681564 - J Biol Chem. 2000 Feb 25;275(8):5767-72 7744969 - J Cell Biol. 1995 May;129(4):979-88 10835343 - EMBO J. 2000 Jun 1;19(11):2444-51 2692852 - Curr Genet. 1989 Dec;16(5-6):339-46 1706459 - Methods Enzymol. 1991;194:398-405 15525670 - Mol Biol Cell. 2005 Jan;16(1):248-59 15119823 - Curr Issues Mol Biol. 2004 Jul;6(2):125-36 9371805 - Proc Natl Acad Sci U S A. 1997 Nov 25;94(24):13093-8 10893257 - J Cell Biol. 2000 Jul 10;150(1):65-76 15053871 - Mol Cell. 2004 Mar 26;13(6):771-81 2225910 - Crit Rev Biochem Mol Biol. 1990;25(4):281-305 12140549 - Nature. 2002 Jul 25;418(6896):387-91 18562668 - Genetics. 2008 Jul;179(3):1301-11 9476895 - Cell. 1998 Feb 6;92(3):351-66 7603990 - Proc Natl Acad Sci U S A. 1995 Jul 3;92(14):6319-23 10480867 - J Biol Chem. 1999 Sep 17;274(38):26654-60 10747017 - EMBO J. 2000 Apr 3;19(7):1486-93 3302682 - Mol Cell Biol. 1987 Jul;7(7):2568-77 |
| References_xml | – volume: 13 start-page: 771 year: 2004 end-page: 781 ident: CR11 article-title: Yeast adapt to near-freezing temperatures by STRE/Msn2,4-dependent induction of trehalose synthesis and certain molecular chaperones publication-title: Mol. Cell doi: 10.1016/S1097-2765(04)00148-0 – volume: 6 start-page: 125 year: 2004 end-page: 136 ident: CR22 article-title: Recent developments in bacterial cold-shock response publication-title: Curr. Issues Mol. Biol. – volume: 25 start-page: 281 year: 1990 end-page: 305 ident: CR23 article-title: Cold denaturation of proteins publication-title: Crit. Rev. Biochem. Mol. Biol. doi: 10.3109/10409239009090612 – volume: 418 start-page: 387 year: 2002 end-page: 391 ident: CR9 article-title: Functional profiling of the genome publication-title: Nature doi: 10.1038/nature00935 – volume: 3 start-page: 51 year: 2009 end-page: 58 ident: CR7 article-title: Molecular chaperones antagonize proteotoxicity by differentially modulating protein aggregation pathways publication-title: Prion doi: 10.4161/pri.3.2.8587 – volume: 94 start-page: 4978 year: 1997 end-page: 4981 ident: CR12 article-title: Trigger factor is induced upon cold shock and enhances viability of at low temperatures publication-title: Proc. Natl. Acad. Sci. USA doi: 10.1073/pnas.94.10.4978 – volume: 33 start-page: 13655 year: 2011 end-page: 13670 ident: CR29 article-title: Single methyl group determines prion propagation and protein degradation activities of yeast heat shock protein (Hsp)-70 chaperones Ssa1p and Ssa2p publication-title: Proc. Natl. Acad. Sci. USA – volume: 143 start-page: 921 year: 1998 end-page: 933 ident: CR30 article-title: A role for the DnaJ homologue Scj1p in protein folding in the yeast endoplasmic reticulum publication-title: J. Cell Biol. doi: 10.1083/jcb.143.4.921 – volume: 275 start-page: 5767 year: 2000 end-page: 5772 ident: CR33 article-title: The assembly factor Atp11p binds to the beta-subunit of the mitochondrial F(1)-ATPase publication-title: J. Biol. Chem. doi: 10.1074/jbc.275.8.5767 – volume: 87 start-page: 4986 year: 1990 end-page: 4990 ident: CR1 article-title: Identification of two nuclear genes (ATP11, ATP12) required for assembly of the yeast F1-ATPase publication-title: Proc. Natl. Acad. Sci. USA doi: 10.1073/pnas.87.13.4986 – volume: 7 start-page: 2568 year: 1987 end-page: 2577 ident: CR35 article-title: Complex interactions among members of an essential subfamily of hsp70 genes in publication-title: Mol. Cell. Biol. – volume: 94 start-page: 12949 year: 1997 end-page: 12956 ident: CR19 article-title: functions of the Hsp90 chaperone publication-title: Proc. Natl. Acad. Sci. USA doi: 10.1073/pnas.94.24.12949 – volume: 169 start-page: 2092 year: 1987 end-page: 2095 ident: CR10 article-title: Induction of proteins in response to low temperature in publication-title: J. Bacteriol. – volume: 16 start-page: 339 year: 1989 end-page: 346 ident: CR24 article-title: High efficiency transformation of intact yeast cells using single stranded nucleic acid as carrier publication-title: Curr. Genet. doi: 10.1007/BF00340712 – volume: 98 start-page: 7313 year: 2001 end-page: 7318 ident: CR32 article-title: Protein misfolding and temperature up-shift cause G1 arrest via a common mechanism dependent on heat shock factor in publication-title: Proc. Natl. Acad. Sci. USA doi: 10.1073/pnas.121172998 – volume: 150 start-page: 65 year: 2000 end-page: 76 ident: CR3 article-title: The heat shock protein Ssa2p is required for import of fructose-1, 6-bisphosphatase into Vid vesicles publication-title: J. Cell Biol. doi: 10.1083/jcb.150.1.65 – volume: 129 start-page: 979 year: 1995 end-page: 988 ident: CR25 article-title: A yeast DnaJ homologue, Scj1p, can function in the endoplasmic reticulum with BiP/Kar2p via a conserved domain that specifies interactions with Hsp70s publication-title: J. Cell Biol. doi: 10.1083/jcb.129.4.979 – volume: 18 start-page: 7353 year: 1998 end-page: 7359 ident: CR17 article-title: Cns1 is an essential protein associated with the hsp90 chaperone complex in that can restore cyclophilin 40-dependent functions in cpr7Δ cells publication-title: Mol. Cell. Biol. – volume: 19 start-page: 2444 year: 2000 end-page: 2451 ident: CR20 article-title: Prohibitins act as a membrane-bound chaperone for the stabilization of mitochondrial proteins publication-title: EMBO J. doi: 10.1093/emboj/19.11.2444 – volume: 33 start-page: D369 year: 2005 end-page: D373 ident: CR8 article-title: PROPHECY — a database for high-resolution phenomics publication-title: Nucleic Acids Res. doi: 10.1093/nar/gki126 – volume: 94 start-page: 13093 year: 1997 end-page: 13098 ident: CR6 article-title: All cyclophilins and FK506 binding proteins are, individually and collectively, dispensable for viability in publication-title: Proc. Natl. Acad. Sci. USA doi: 10.1073/pnas.94.24.13093 – volume: 7 start-page: 385 year: 2006 end-page: 389 ident: CR5 article-title: Psychrophilic microorganisms: challenges for life publication-title: EMBO Reports doi: 10.1038/sj.embor.7400662 – volume: 19 start-page: 1486 year: 2000 end-page: 1493 ident: CR34 article-title: The alpha-subunit of the mitochondrial F(1)-ATPase interacts directly with the assembly factor Atp12p publication-title: EMBO J. doi: 10.1093/emboj/19.7.1486 – volume: 58 start-page: 157 year: 2009 end-page: 165 ident: CR26 article-title: Intracellular ice formation in yeast cells publication-title: cooling rate: predictions from modeling vs. experimental observations by differential scanning calorimetry. Cryobiology – volume: 92 start-page: 351 year: 1998 end-page: 366 ident: CR4 article-title: The Hsp70 and Hsp60 chaperone machines publication-title: Cell doi: 10.1016/S0092-8674(00)80928-9 – volume: 16 start-page: 248 year: 2005 end-page: 259 ident: CR31 article-title: Formation of membrane-bound ring complexes by prohibitins in mitochondria publication-title: Mol. Biol. Cell doi: 10.1091/mbc.E04-09-0807 – volume: 191 start-page: 805 year: 2012 end-page: 814 ident: CR36 article-title: Chaperoning the chaperone: A role for the co-chaperone Cpr7 in modulating Hsp90 function in publication-title: Genetics doi: 10.1534/genetics.112.140319 – volume: 54 start-page: 1 year: 2008 end-page: 11 ident: CR27 article-title: The Hsp110 protein chaperone Sse1 is required for yeast cell wall integrity and morphogenesis publication-title: Curr. Genet. doi: 10.1007/s00294-008-0193-y – volume: 90 start-page: 5450 year: 1993 end-page: 5454 ident: CR21 article-title: The FKB2 gene of , encoding the immunosuppressant-binding protein FKBP-13, is regulated in response to accumulation of unfolded proteins in the endoplasmic reticulum publication-title: Proc. Natl. Acad. Sci. USA doi: 10.1073/pnas.90.12.5450 – volume: 92 start-page: 6319 year: 1995 end-page: 6323 ident: CR18 article-title: Cyclophilin catalyzes protein folding in yeast mitochondria publication-title: Proc. Natl. Acad. Sci. USA doi: 10.1073/pnas.92.14.6319 – volume: 29 start-page: 567 year: 2010 end-page: 574 ident: CR14 article-title: A cyclophilin A CPR1 over-expression enhances stress acquisition in publication-title: Mol. Cells doi: 10.1007/s10059-010-0071-6 – volume: 194 start-page: 398 year: 1991 end-page: 405 ident: CR15 article-title: Preparation of high molecular weight RNA publication-title: Meth. Enzymol. doi: 10.1016/0076-6879(91)94030-G – volume: 274 start-page: 26654 year: 1999 end-page: 26660 ident: CR16 article-title: The yeast Hsp110 family member, Sse1, is an Hsp90 cochaperone publication-title: J. Biol. Chem. doi: 10.1074/jbc.274.38.26654 – volume: 99 start-page: 8778 year: 2002 end-page: 8783 ident: CR2 article-title: Transcriptional response of to DNA-damaging agents does not identify the genes that protect against these agents publication-title: Proc. Natl. Acad. Sci. USA doi: 10.1073/pnas.132275199 – volume: 16 start-page: 1 year: 2011 end-page: 14 ident: CR13 article-title: Decarbonylated cyclophilin A Cpr1 protein protects KNU5377Y when exposed to stress induced by menadione publication-title: Cell Stress Chaperones doi: 10.1007/s12192-010-0215-9 – volume: 179 start-page: 1301 year: 2008 end-page: 1311 ident: CR28 article-title: Functionally redundant isoforms of a yeast Hsp70 chaperone subfamily have different antiprion effects publication-title: Genetics doi: 10.1534/genetics.108.089458 – volume: 92 start-page: 6319 year: 1995 ident: 2411_CR18 publication-title: Proc. Natl. Acad. Sci. USA doi: 10.1073/pnas.92.14.6319 – volume: 19 start-page: 2444 year: 2000 ident: 2411_CR20 publication-title: EMBO J. doi: 10.1093/emboj/19.11.2444 – volume: 129 start-page: 979 year: 1995 ident: 2411_CR25 publication-title: J. Cell Biol. doi: 10.1083/jcb.129.4.979 – volume: 16 start-page: 339 year: 1989 ident: 2411_CR24 publication-title: Curr. Genet. doi: 10.1007/BF00340712 – volume: 29 start-page: 567 year: 2010 ident: 2411_CR14 publication-title: Mol. Cells doi: 10.1007/s10059-010-0071-6 – volume: 94 start-page: 12949 year: 1997 ident: 2411_CR19 publication-title: Proc. Natl. Acad. Sci. USA doi: 10.1073/pnas.94.24.12949 – volume: 169 start-page: 2092 year: 1987 ident: 2411_CR10 publication-title: J. Bacteriol. doi: 10.1128/jb.169.5.2092-2095.1987 – volume: 418 start-page: 387 year: 2002 ident: 2411_CR9 publication-title: Nature doi: 10.1038/nature00935 – volume: 54 start-page: 1 year: 2008 ident: 2411_CR27 publication-title: Curr. Genet. doi: 10.1007/s00294-008-0193-y – volume: 25 start-page: 281 year: 1990 ident: 2411_CR23 publication-title: Crit. Rev. Biochem. Mol. Biol. doi: 10.3109/10409239009090612 – volume: 194 start-page: 398 year: 1991 ident: 2411_CR15 publication-title: Meth. Enzymol. doi: 10.1016/0076-6879(91)94030-G – volume: 18 start-page: 7353 year: 1998 ident: 2411_CR17 publication-title: Mol. Cell. Biol. doi: 10.1128/MCB.18.12.7353 – volume: 7 start-page: 385 year: 2006 ident: 2411_CR5 publication-title: EMBO Reports doi: 10.1038/sj.embor.7400662 – volume: 98 start-page: 7313 year: 2001 ident: 2411_CR32 publication-title: Proc. Natl. Acad. Sci. USA doi: 10.1073/pnas.121172998 – volume: 179 start-page: 1301 year: 2008 ident: 2411_CR28 publication-title: Genetics doi: 10.1534/genetics.108.089458 – volume: 3 start-page: 51 year: 2009 ident: 2411_CR7 publication-title: Prion doi: 10.4161/pri.3.2.8587 – volume: 6 start-page: 125 year: 2004 ident: 2411_CR22 publication-title: Curr. Issues Mol. Biol. – volume: 33 start-page: 13655 year: 2011 ident: 2411_CR29 publication-title: Proc. Natl. Acad. Sci. USA – volume: 150 start-page: 65 year: 2000 ident: 2411_CR3 publication-title: J. Cell Biol. doi: 10.1083/jcb.150.1.65 – volume: 33 start-page: D369 year: 2005 ident: 2411_CR8 publication-title: Nucleic Acids Res. doi: 10.1093/nar/gki126 – volume: 87 start-page: 4986 year: 1990 ident: 2411_CR1 publication-title: Proc. Natl. Acad. Sci. USA doi: 10.1073/pnas.87.13.4986 – volume: 58 start-page: 157 year: 2009 ident: 2411_CR26 publication-title: cooling rate: predictions from modeling vs. experimental observations by differential scanning calorimetry. Cryobiology – volume: 7 start-page: 2568 year: 1987 ident: 2411_CR35 publication-title: Mol. Cell. Biol. doi: 10.1128/MCB.7.7.2568 – volume: 13 start-page: 771 year: 2004 ident: 2411_CR11 publication-title: Mol. Cell doi: 10.1016/S1097-2765(04)00148-0 – volume: 143 start-page: 921 year: 1998 ident: 2411_CR30 publication-title: J. Cell Biol. doi: 10.1083/jcb.143.4.921 – volume: 94 start-page: 4978 year: 1997 ident: 2411_CR12 publication-title: Proc. Natl. Acad. Sci. USA doi: 10.1073/pnas.94.10.4978 – volume: 90 start-page: 5450 year: 1993 ident: 2411_CR21 publication-title: Proc. Natl. Acad. Sci. USA doi: 10.1073/pnas.90.12.5450 – volume: 19 start-page: 1486 year: 2000 ident: 2411_CR34 publication-title: EMBO J. doi: 10.1093/emboj/19.7.1486 – volume: 99 start-page: 8778 year: 2002 ident: 2411_CR2 publication-title: Proc. Natl. Acad. Sci. USA doi: 10.1073/pnas.132275199 – volume: 92 start-page: 351 year: 1998 ident: 2411_CR4 publication-title: Cell doi: 10.1016/S0092-8674(00)80928-9 – volume: 16 start-page: 248 year: 2005 ident: 2411_CR31 publication-title: Mol. Biol. Cell doi: 10.1091/mbc.E04-09-0807 – volume: 94 start-page: 13093 year: 1997 ident: 2411_CR6 publication-title: Proc. Natl. Acad. Sci. USA doi: 10.1073/pnas.94.24.13093 – volume: 16 start-page: 1 year: 2011 ident: 2411_CR13 publication-title: Cell Stress Chaperones doi: 10.1007/s12192-010-0215-9 – volume: 275 start-page: 5767 year: 2000 ident: 2411_CR33 publication-title: J. Biol. Chem. doi: 10.1074/jbc.275.8.5767 – volume: 191 start-page: 805 year: 2012 ident: 2411_CR36 publication-title: Genetics doi: 10.1534/genetics.112.140319 – volume: 274 start-page: 26654 year: 1999 ident: 2411_CR16 publication-title: J. Biol. Chem. doi: 10.1074/jbc.274.38.26654 – reference: 10835343 - EMBO J. 2000 Jun 1;19(11):2444-51 – reference: 10681564 - J Biol Chem. 2000 Feb 25;275(8):5767-72 – reference: 22505624 - Genetics. 2012 Jul;191(3):805-14 – reference: 20680535 - Cell Stress Chaperones. 2011 Jan;16(1):1-14 – reference: 20496120 - Mol Cells. 2010 Jun;29(6):567-74 – reference: 18478233 - Curr Genet. 2008 Jul;54(1):1-11 – reference: 16585939 - EMBO Rep. 2006 Apr;7(4):385-9 – reference: 10480867 - J Biol Chem. 1999 Sep 17;274(38):26654-60 – reference: 12077312 - Proc Natl Acad Sci U S A. 2002 Jun 25;99(13):8778-83 – reference: 9819422 - Mol Cell Biol. 1998 Dec;18(12):7353-9 – reference: 15053871 - Mol Cell. 2004 Mar 26;13(6):771-81 – reference: 7685904 - Proc Natl Acad Sci U S A. 1993 Jun 15;90(12):5450-4 – reference: 2225910 - Crit Rev Biochem Mol Biol. 1990;25(4):281-305 – reference: 9476895 - Cell. 1998 Feb 6;92(3):351-66 – reference: 10747017 - EMBO J. 2000 Apr 3;19(7):1486-93 – reference: 10893257 - J Cell Biol. 2000 Jul 10;150(1):65-76 – reference: 7744969 - J Cell Biol. 1995 May;129(4):979-88 – reference: 19421006 - Prion. 2009 Apr-Jun;3(2):51-8 – reference: 2692852 - Curr Genet. 1989 Dec;16(5-6):339-46 – reference: 3302682 - Mol Cell Biol. 1987 Jul;7(7):2568-77 – reference: 19118541 - Cryobiology. 2009 Apr;58(2):157-65 – reference: 2142305 - Proc Natl Acad Sci U S A. 1990 Jul;87(13):4986-90 – reference: 15608218 - Nucleic Acids Res. 2005 Jan 1;33(Database issue):D369-73 – reference: 21808014 - Proc Natl Acad Sci U S A. 2011 Aug 16;108(33):13665-70 – reference: 9371781 - Proc Natl Acad Sci U S A. 1997 Nov 25;94(24):12949-56 – reference: 9144175 - Proc Natl Acad Sci U S A. 1997 May 13;94(10):4978-81 – reference: 12140549 - Nature. 2002 Jul 25;418(6896):387-91 – reference: 18562668 - Genetics. 2008 Jul;179(3):1301-11 – reference: 9817751 - J Cell Biol. 1998 Nov 16;143(4):921-33 – reference: 15119823 - Curr Issues Mol Biol. 2004 Jul;6(2):125-36 – reference: 11416208 - Proc Natl Acad Sci U S A. 2001 Jun 19;98 (13):7313-8 – reference: 7603990 - Proc Natl Acad Sci U S A. 1995 Jul 3;92(14):6319-23 – reference: 3553157 - J Bacteriol. 1987 May;169(5):2092-5 – reference: 9371805 - Proc Natl Acad Sci U S A. 1997 Nov 25;94(24):13093-8 – reference: 1706459 - Methods Enzymol. 1991;194:398-405 – reference: 15525670 - Mol Biol Cell. 2005 Jan;16(1):248-59 |
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| Title | Identification of Chaperones in Freeze Tolerance in Saccharomyces cerevisiae |
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| ispartofPNX | The Journal of Microbiology, 2012, 50(5), , pp.882-887 |
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