RT Journal
A1 Hu, Yanhui
A1 Rolfs, Andreas
A1 Bhullar, Bhupinder
A1 Murthy, Tellamraju V. S.
A1 Zhu, Cong
A1 Berger, Michael F.
A1 Camargo, Anamaria A.
A1 Kelley, Fontina
A1 McCarron, Seamus
A1 Jepson, Daniel
A1 Richardson, Aaron
A1 Raphael, Jacob
A1 Moreira, Donna
A1 Taycher, Elena
A1 Zuo, Dongmei
A1 Mohr, Stephanie
A1 Kane, Michael F.
A1 Williamson, Janice
A1 Simpson, Andrew
A1 Bulyk, Martha L.
A1 Harlow, Edward
A1 Marsischky, Gerald
A1 Kolodner, Richard D.
A1 LaBaer, Joshua
T1 Approaching a complete repository of sequence-verified protein-encoding clones for Saccharomyces cerevisiae
JF Genome Research 
JO Genome Research 
YR 2007 
FD April 01 
VO 17 
IS 4 
SP 000 
OP 000 
DO 10.1101/gr.6037607 
UL http://genome.cshlp.org/content/early/2007/02/23/gr.6037607.abstract 
AB The availability of an annotated genome sequence for the yeast Saccharomyces cerevisiae has made possible the proteome-scale study of protein function and protein–protein interactions. These studies rely on availability of cloned open reading frame (ORF) collections that can be used for cell-free or cell-based protein expression. Several yeast ORF collections are available, but their use and data interpretation can be hindered by reliance on now out-of-date annotations, the inflexible presence of N- or C-terminal tags, and/or the unknown presence of mutations introduced during the cloning process. High-throughput biochemical and genetic analyses would benefit from a “gold standard” (fully sequence-verified, high-quality) ORF collection, which allows for high confidence in and reproducibility of experimental results. Here, we describe Yeast FLEXGene, a S. cerevisiae protein-coding clone collection that covers over 5000 predicted protein-coding sequences. The clone set covers 87% of the current S. cerevisiae genome annotation and includes full sequencing of each ORF insert. Availability of this collection makes possible a wide variety of studies from purified proteins to mutation suppression analysis, which should contribute to a global understanding of yeast protein function.