Biochemical and genetic analysis of the yeast proteome with a movable ORF collection

Functional analysis of the proteome is an essential part of genomic research. To facilitate different proteomic approaches, a MORF (moveable ORF) library of 5854 yeast expression plasmids was constructed, each expressing a sequence-verified ORF as a C-terminal ORF fusion protein, under regulated con...

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Published inGenes & development Vol. 19; no. 23; pp. 2816 - 2826
Main Authors Gelperin, Daniel M, White, Michael A, Wilkinson, Martha L, Kon, Yoshiko, Kung, Li A, Wise, Kevin J, Lopez-Hoyo, Nelson, Jiang, Lixia, Piccirillo, Stacy, Yu, Haiyuan, Gerstein, Mark, Dumont, Mark E, Phizicky, Eric M, Snyder, Michael, Grayhack, Elizabeth J
Format Journal Article
LanguageEnglish
Published United States Cold Spring Harbor Laboratory Press 01.12.2005
Subjects
Cell Growth Processes - genetics
Fungal Proteins - analysis
Fungal Proteins - genetics
Gene Library
Glycoproteins - analysis
Glycoproteins - genetics
Open Reading Frames
Proteome
Proteomics - methods
Research Papers
Yeasts - genetics
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Abstract Functional analysis of the proteome is an essential part of genomic research. To facilitate different proteomic approaches, a MORF (moveable ORF) library of 5854 yeast expression plasmids was constructed, each expressing a sequence-verified ORF as a C-terminal ORF fusion protein, under regulated control. Analysis of 5573 MORFs demonstrates that nearly all verified ORFs are expressed, suggests the authenticity of 48 ORFs characterized as dubious, and implicates specific processes including cytoskeletal organization and transcriptional control in growth inhibition caused by overexpression. Global analysis of glycosylated proteins identifies 109 new confirmed N-linked and 345 candidate glycoproteins, nearly doubling the known yeast glycome.
AbstractList Functional analysis of the proteome is an essential part of genomic research. To facilitate different proteomic approaches, a MORF (moveable ORF) library of 5854 yeast expression plasmids was constructed, each expressing a sequence-verified ORF as a C-terminal ORF fusion protein, under regulated control. Analysis of 5573 MORFs demonstrates that nearly all verified ORFs are expressed, suggests the authenticity of 48 ORFs characterized as dubious, and implicates specific processes including cytoskeletal organization and transcriptional control in growth inhibition caused by overexpression. Global analysis of glycosylated proteins identifies 109 new confirmed N-linked and 345 candidate glycoproteins, nearly doubling the known yeast glycome.
Author Kon, Yoshiko
Dumont, Mark E
Snyder, Michael
Yu, Haiyuan
Wise, Kevin J
Jiang, Lixia
Gerstein, Mark
Phizicky, Eric M
Lopez-Hoyo, Nelson
Gelperin, Daniel M
Wilkinson, Martha L
Piccirillo, Stacy
White, Michael A
Grayhack, Elizabeth J
Kung, Li A
AuthorAffiliation 1 Department of Biochemistry and Biophysics, University of Rochester School of Medicine and Dentistry, Rochester, New York 14642, USA; 2 Department of Molecular, Cellular, and Developmental Biology, and 3 Department of Biochemistry and Biophysics, Yale University, New Haven, Connecticut 06520, USA
AuthorAffiliation_xml – name: 1 Department of Biochemistry and Biophysics, University of Rochester School of Medicine and Dentistry, Rochester, New York 14642, USA; 2 Department of Molecular, Cellular, and Developmental Biology, and 3 Department of Biochemistry and Biophysics, Yale University, New Haven, Connecticut 06520, USA
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  surname: Gelperin
  fullname: Gelperin, Daniel M
  organization: Department of Biochemistry and Biophysics, University of Rochester School of Medicine and Dentistry, Rochester, New York 14642, USA
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  surname: White
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BackLink https://www.ncbi.nlm.nih.gov/pubmed/16322557$$D View this record in MEDLINE/PubMed
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content type line 23
These authors contributed equally to this work.
Supplemental material is available at http://www.genesdev.org.
E-MAIL elizabeth_grayhack@urmc.rochester.edu ; FAX (585) 271-2683.
E-MAIL michael.snyder@yale.edu ; FAX (203) 432-3597.
Corresponding authors.
Article and publication are at http://www.genesdev.org/cgi/doi/10.1101/gad.1362105.
OpenAccessLink http://genesdev.cshlp.org/content/19/23/2816.full.pdf
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Proteome
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