RAT-LIVER DNA LIGASES - CATALYTIC PROPERTIES OF A NOVEL FORM OF DNA-LIGASE

被引:27
作者
ELDER, RH
MONTECUCCO, A
CIARROCCHI, G
ROSSIGNOL, JM
机构
[1] INST RECH SCI CANC,CNRS,BIOL MOLEC REPLICAT LAB,UPR 272,BP 8,F-94802 VILLEJUIF,FRANCE
[2] CNR,IST GENET BIOCHEM & EVOLUZIONIST,PAVIA,ITALY
来源
EUROPEAN JOURNAL OF BIOCHEMISTRY | 1992年 / 203卷 / 1-2期
关键词
D O I
10.1111/j.1432-1033.1992.tb19826.x
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
A novel form of rat liver DNA ligase (molecular mass 100 kDa) can be differentiated from DNA ligase I by several biochemical parameters. It is a more heat-labile enzyme and unable to join blunt-ended DNA, even in the presence of poly(ethylene glycol) concentrations which stimulate such joining by DNA ligase I and T4 DNA ligase. It also lacks the AMP-dependent nicking/closing reaction, which is a property of all other DNA ligases tested so far, including DNA ligase I from rat liver. Both rat liver DNA ligases were inhibited by deoxyadenosinetriphosphate, however this inhibition was competitive with respect to ATP, for DNA ligase I (K(i) 22-mu-M) and non-competitive for the 100-kDa DNA ligase (K(i) 170-mu-M). These results support the idea that, when compared with other DNA ligases, the novel form of DNA ligase has a unique AMP-binding site, may have an absolute requirement for single-strand breaks and, furthermore, may have an altered reaction mechanism to that which is conserved from bacteriophage to mammalian DNA ligase I.
引用
收藏
页码:53 / 58
页数:6
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