RRC ID 21414
Author Hou J, Liu Y, Lu Z, Liu X, Liu J.
Title Biochemical characterization of RNase HII from Aeropyrum pernix.
Journal Acta Biochim Biophys Sin (Shanghai)
Abstract Aeropyrum pernix contains one homolog of ribonuclease H (RNase H), A. pernix RNase HII (Ape-RNase HII). Activity characterization showed that Ape-RNase HII exhibited the highest activity in the presence of 5 mM Mn(2+), 1 mM Co(2+), or 10 mM Mg(2+), respectively; however, its cleavage efficiencies at different cleavage sites for Mn(2+) and Mg(2+) were different. Ape-RNase HII cleaved 12-bp RNA/DNA substrates at multiple sites and the optimum pH value was 11.0. Moreover, 16-bp DNA-r4-DNA/DNA and 13-bp DNA-r1-DNA/DNA chimeric substrates were cleaved at DNA-RNA junction. Ape-RNase HII was thermostable and the stabilization was enhanced with increased salt concentration. This work is believed to be the first in vitro functional study of Ape-RNase HII and the results should contribute to the analysis of RNase H of other archaeal species.
Volume 44(4)
Pages 339-46
Published 2012-4-1
DOI 10.1093/abbs/gms011
PII gms011
PMID 22366566
MeSH Aeropyrum / enzymology* Aeropyrum / genetics Amino Acid Sequence Archaeal Proteins / genetics Archaeal Proteins / metabolism* Binding Sites / genetics Biocatalysis / drug effects Cobalt / pharmacology DNA, Archaeal / genetics DNA, Archaeal / metabolism Electrophoresis, Polyacrylamide Gel Enzyme Stability Hydrogen-Ion Concentration Kinetics Manganese / pharmacology Molecular Sequence Data RNA, Archaeal / genetics RNA, Archaeal / metabolism Recombinant Proteins / metabolism Ribonuclease H / genetics Ribonuclease H / metabolism* Sequence Homology, Amino Acid Substrate Specificity Temperature
IF 2.836
Times Cited 6
WOS Category BIOPHYSICS BIOCHEMISTRY & MOLECULAR BIOLOGY
Resource
General Microbes JCM 9820