RNA ligase of bacteriophage RM 378

The use of thermophilic enzymes has revolutionized the field of recombinant DNA technology. Polymerases (DNA and RNA), ligases, exonucleases, reverse transcriptases, polynucleotide kinases and lysozymes, as well as many other thermophilic enzymes, are of great importance in the research industry tod...

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Main Authors Hjörleifsdottir, Sigridur, Hreggvidsson, Gudmundur O, Fridjonsson, Olafur H, Aevarsson, Arnthor, Kristjansson, Jakob K
Format Patent
LanguageEnglish
Published 16.11.2004
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Abstract The use of thermophilic enzymes has revolutionized the field of recombinant DNA technology. Polymerases (DNA and RNA), ligases, exonucleases, reverse transcriptases, polynucleotide kinases and lysozymes, as well as many other thermophilic enzymes, are of great importance in the research industry today. In addition, thermophilic enzymes are also used in commercial settings (e.g., proteases and lipases used in washing powder, hydrolidic enzymes used in bleaching). Identification of new thermophilic enzymes will facilitate continued DNA research as well as assist in improving commercial enzyme-based products. A novel bacteriophage RM 378 of , the nucleic acids of its genome, nucleic acids comprising nucleotide sequences of open reading frames (ORFs) of its genome, and polypeptides encoded by the nucleic acids, are described.
AbstractList The use of thermophilic enzymes has revolutionized the field of recombinant DNA technology. Polymerases (DNA and RNA), ligases, exonucleases, reverse transcriptases, polynucleotide kinases and lysozymes, as well as many other thermophilic enzymes, are of great importance in the research industry today. In addition, thermophilic enzymes are also used in commercial settings (e.g., proteases and lipases used in washing powder, hydrolidic enzymes used in bleaching). Identification of new thermophilic enzymes will facilitate continued DNA research as well as assist in improving commercial enzyme-based products. A novel bacteriophage RM 378 of , the nucleic acids of its genome, nucleic acids comprising nucleotide sequences of open reading frames (ORFs) of its genome, and polypeptides encoded by the nucleic acids, are described.
Author Hreggvidsson, Gudmundur O
Aevarsson, Arnthor
Fridjonsson, Olafur H
Kristjansson, Jakob K
Hjörleifsdottir, Sigridur
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References Rand et al. The EMBO Journal. 1984; 3 (2): 397-402.
Moreira, L., et al., "Genomic Typing and Fatty Acid Composition of Rhodothermus marinus", Syst. Appl. Microbiol., 19(1):83-90 (1996).
Hopfner Karl-Peter et al., "Crystal Structure of a Thermostable Type B DNA Polymerase From Thermococcus gorgonarius," Proc. Nat. Acad. of Sci., 96(7): 3600-3605 (1999).
Andresson, O.S. and Fridjonsson, O.H., "The Sequence of the Single 16S rRNA Gene of the Thermophilic Eubacterium Rhodothermus marinus Reveals a Distant Relationship to the Group Containing Flexibacter, Bacteroides, and Cytophaga Species", J. Bacteriol., 176(19):6165-6169 (1994).
Wang, J. et al., "Crystal Structure of a Pol Family Replication DNA Polymerase from Bacteriophage RB69," Cell, 89(7): 1087-1099 (1997).
Pisani, F.M., et al., "Amino Acid Residues Involved in Determining the Processivity of the 3′-5′ Exonuclease Activity in a Family B DNA Polymerase from the Thermoacidophilic Archaeon Sulfolobus solfataricus," Biochem. 37(42): 15005-15012 (1998).
Barnes (5436149) 19950700
"DNA Polymerase I, Klenow (Exonuclease-Free)," Mol. Bio. Reagents, 88 (XP000606205), (1990).
Alfredsson, G.A., et al., "Rhodothermus marinus, gen. nov., sp. nov., a Thermophilic Halophilic Bacterium from Submarine Hot Springs in Iceland", J. Gen. Microbiol., 134(Pt. 2):299-306 (1988).
Hjörleifsdottir (6492161) 20021200
"Exonuclease III (E. Coli)," New England Biolabs Catalog, 94 (XP002164084) 1998-1999.
"DNA polymerase and formulations comprising it-allowing the amplification of sequences up to 35 kilobases and reducing the mutagenicity generated by the PCR process." WPI Acc No. 1995-006692/199501 (Abstract).
(WO94 26766) 19941100
Durantel et al. Journal of General Virology. Mar., 1998; 79: 629-637.
Shuman et al. PNAS. 1994; 91: 12046-12050.
Blondal et al. Nucleic Acids Research. Dec. 15, 2003; 31 (24): 7247-54.
Cong et al. Journal of Biological Chemistry. 1993; 268 (10): 7256-7260.
Nunes, O.C., et al., "Isolation and Characterization of Rhodothermus Strains from S. Miguel, Azores", Syst. Appl. Microbiol., 15(1):92-97 (1992).
Cong et al. Molecular and Cellular Biology. 1995; 15 (11): 6222-6231.
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