Open AccessPurification and crystallization of RNase HIII from Staphylococcus aureus
Author(s) -
Reiling Scott A.,
Homma Kohei,
Asojo Oluwatoyin A.
Publication year - 2011
Publication title -
acta crystallographica section f
Language(s) - English
Resource type - Journals
ISSN - 1744-3091
DOI - 10.1107/s1744309110045616
Subject(s) - rnase mrp , rnase h , rnase p , biology , staphylococcus aureus , dna , rna , genetics , microbiology and biotechnology , bacteria , gene
As part of collaborative efforts to characterize virulence factors from Staphylococcus aureus , methods for the large‐scale recombinant production of RNase HIII from S. aureus subspecies MRSA252 (Sa‐RNase HIII) have been developed. RNase HIII‐type ribonucleases are poorly characterized members of the RNase H group of endonucleases which hydrolyze RNA from RNA/DNA hybrids and are thought to be involved in DNA replication and repair. They are characterized by N‐terminal extensions of unknown function that do not share sequence homology with the N‐terminal extensions of bacterial RNases HI and RNases HII. Sa‐RNase HIII was crystallized in the orthorhombic space group P 2 1 2 1 2 1 , with unit‐cell parameters a = 48.9, b = 74.2, c = 127.5 Å, and diffracted to 2.6 Å resolution.