Genomic analysis of biochemical function.
Establishing the linkage between an individual biochemical activity and the gene(s) specifying that activity has been facilitated by advances in mass spectrometry and affinity purification methods. In addition, a genomic protein array has been produced in yeast by fusing each yeast open reading frame to glutathione-S-transferase, thus linking each protein with its cognate gene. Purification and biochemical assay of pools of glutathione-S-transferase-open-reading-frame proteins allows analysis of the entire proteome for biochemical activities, followed by simple deconvolution to identify the responsible open reading frame. An alternative method to analyze large sets of proteins is the use of protein microarrays in which over 10,000 individual proteins can be immobilized and assayed on a single slide.
Grayhack
E J
EJ
Department of Biochemistry and Biophysics, University of Rochester, School of Medicine and Dentistry, 601 Elmwood Avenue, Box 712, Rochester, NY 14642, USA. elizabeth_grayhack@urmc.rochester.edu
Phizicky
E M
EM
D000818:Animals; D001709:Biotechnology / Q000379:methods; D016678:Genome; D006801:Humans; D016366:Open Reading Frames / Q000235:genetics; D011506:Proteins / Q000032:analysis* / Q000235:genetics* / Q000494:pharmacology; D011993:Recombinant Fusion Proteins / Q000235:genetics; D012371:Robotics
D011506:Proteins; D011993:Recombinant Fusion Proteins