Systematic deletion analysis of fission yeast protein kinases

被引:84
作者
Bimbó, A
Jia, YH
Poh, SL
Karuturi, RKM
den Elzen, N
Peng, X
Zheng, LL
O'Connell, M
Liu, ET
Balasubramanian, MK
Liu, JH
机构
[1] Natl Univ Singapore, Temasek Life Sci Lab, Singapore 117604, Singapore
[2] Genome Inst Singapore, Singapore 138672, Singapore
[3] Peter MacCallum Canc Ctr, Melbourne, Vic 3002, Australia
[4] Natl Univ Singapore, Dept Biol Sci, Singapore 117548, Singapore
[5] Natl Univ Singapore, Dept Biochem, Singapore 117548, Singapore
关键词
D O I
10.1128/EC.4.4.799-813.2005
中图分类号
Q93 [微生物学];
学科分类号
071005 ; 100705 ;
摘要
Eukaryotic protein kinases are key molecules mediating signal transduction that play a pivotal role in the regulation of various biological processes, including cell cycle progression, cellular morphogenesis, development, and cellular response to environmental changes. A total of 106 eukaryotic protein kinase catalytic-domain-containing proteins have been found in the entire fission yeast genome, 44% (or 64%) of which possess orthologues (or nearest homologues) in humans, based on sequence similarity within catalytic domains. Systematic deletion analysis of all putative protein kinase-encoding genes have revealed that 17 out of 106 were essential for viability, including three previously uncharacterized putative protein kinases. Although the remaining 89 protein kinase mutants were able to form colonies under optimal growth conditions, 46% of the mutants exhibited hypersensitivity to at least 1 of the 17 different stress factors tested. Phenotypic assessment of these mutants allowed us to arrange kinases into functional groups. Based on the results of this assay, we propose also the existence of four major signaling pathways that are involved in the response to 17 stresses tested. Microarray analysis demonstrated a significant correlation between the expression signature and growth phenotype of kinase mutants tested. Our complete microarray data sets are available at http://giscompute.gis.a-star.edu.sg/similar to gisljh/kinome.
引用
收藏
页码:799 / 813
页数:15
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