Yeast RNase H(35) is the counterpart of the mammalian RNase HI, and is evolutionarily related to prokaryotic RNase HII

FEBS Letters

Braunshofer-Reiter, Christa¹  Frank, Peter¹  Wintersberger, Ulrike¹ 

[1] Department of Molecular Genetics, Institute of Tumor Biology and Cancer Research, University of Vienna, Borschkegasse 8a, A-1090 Vienna, Austria

关键词: Ribonuclease H;    RNA-DNA hybrid;    Saccharomyces cerevisiae;    Mammalia;    Escherichia coli;    Evolution;    RNase H;    ribonuclease H;    ORF;    open reading frame;    PCR;    polymerase chain reaction;    IPTG;    isopropyl-1-thio-β-d-galactopyranoside;    SDS-PAGE;    sodium dodecyl sulfate-polyacrylamide gel electrophoresis;    PMSF;    phenylmethylsulfonyl fluoride;   

DOI  :  10.1016/S0014-5793(97)01528-7

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

We cloned the Saccharomyces cerevisiae homologue of mammalian RNase HI, which itself is related to the prokaryotic RNase HII, an enzyme of unknown function and previously described as having minor activity in Escherichia coli. Expression of the corresponding yeast 35 kDa protein (named by us RNase H(35)) in E. coli and immunological analysis proves a close evolutionary relationship to mammalian RNase HI. Deletion of the gene (called RNH35) from the yeast genome leads to an about 75% decrease of RNase H activity in preparations from the mutated, still viable cells. Sequence comparison discriminates this new yeast RNase H from earlier described yeast enzymes, RNase H(70) and RNase HI.

【 授权许可】

Unknown