Protein sequences conserved in prokaryotic aminoacyl-tRNA synthetases are important for the activity of the processivity factor of human mitochondrial DNA polymerase

被引:38
作者
Carrodeguas, JA [1 ]
Bogenhagen, DF [1 ]
机构
[1] SUNY Stony Brook, Dept Pharmacol Sci, Stony Brook, NY 11794 USA
关键词
D O I
10.1093/nar/28.5.1237
中图分类号
Q5 [生物化学]; Q7 [分子生物学];
学科分类号
071010 ; 081704 ;
摘要
Previous studies have shown that the small subunit of Xenopus DNA polymerase gamma (pol gamma B) acts as a processivity factor to stimulate the 140 kDa catalytic subunit of human DNA polymerase gamma, A putative human pol gamma B initially identified by analysis of DNA sequence had not been shown to be functional, and appeared to be an incomplete clone. In this paper, we report the cloning of full-length human and mouse pol gamma B, Both human and mouse pol gamma B proteins were expressed in their mature forms, without their apparent mitochondrial localization signals, and shown to stimulate processivity of the recombinant catalytic subunit of human pol gamma A. Deletion analysis of human pol gamma B indicated that blocks of sequence conserved with prokaryotic class II aminoacyl-tRNA synthetases are necessary for activity and interaction with human pol gamma A. Purification of DNA pol gamma from HeLa cells indicated that both proteins are associated in vivo.
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页码:1237 / 1244
页数:8
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