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Purification and crystallization of RNase HIII from Staphylococcus aureus.

ABSTRACT: 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 P2(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.

SUBMITTER: Reiling SA

PROVIDER: S-EPMC3079978 | biostudies-literature | 2011 Jan

REPOSITORIES: biostudies-literature

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Purification and crystallization of RNase HIII from Staphylococcus aureus.

Reiling Scott A SA Homma Kohei K Asojo Oluwatoyin A OA

Acta crystallographica. Section F, Structural biology and crystallization communications 20101222 Pt 1

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 functi ...[more]

PMID: 21206030

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