NDLI: Identification of Amino Acid Residues Critical for Catalysis of Holliday Junction Resolution by Mycoplasma genitalium RecU ▿

Content Provider	PubMed Central
Author	Sluijter, Marcel Aslam, Md Hartwig, Nico G. Rossum, Annemarie M. C. Van Vink, Cornelis
Copyright Year	2011
Abstract	The RecU protein from Mycoplasma genitalium, RecU Mge , is a 19.4-kDa Holliday junction (HJ) resolvase that binds in a nonspecific fashion to HJ substrates and, in the presence of Mn2+, cleaves these substrates at a specific sequence (5′-G/TC↓C/TTA/GG-3′). To identify amino acid residues that are crucial for HJ binding and/or cleavage, we generated a series of 16 deletion mutants (9 N- and 7 C-terminal deletion mutants) and 31 point mutants of RecU Mge . The point mutations were introduced at amino acid positions that are highly conserved among bacterial RecU-like sequences. All mutants were purified and tested for the ability to bind to, and cleave, HJ substrates. We found the five N-terminal and three C-terminal amino acid residues of RecU Mge to be dispensable for its catalytic activities. Among the 31 point mutants, 7 mutants were found to be inactive in both HJ binding and cleavage. Interestingly, in 12 other mutants, these two activities were uncoupled; while these proteins displayed HJ-binding characteristics similar to those of wild-type RecU Mge , they were unable to cleave HJ substrates. Thus, 12 amino acid residues were identified (E11, K31, D57, Y58, Y66, D68, E70, K72, T74, K76, Q88, and L92) that may play either a direct or indirect role in the catalysis of HJ resolution.
Related Links	http://dx.doi.org/10.1128/jb.00247-11
Ending Page	3948
Page Count	8
Starting Page	3941
File Format	PDF
ISSN	00219193
e-ISSN	10985530
Journal	Journal of Bacteriology
Issue Number	15
Volume Number	193
Language	English
Publisher	American Society for Microbiology
Publisher Date	2011-08-01
Access Restriction	Open
Rights Holder	American Society for Microbiology
Subject Keyword	Molecular Biology Microbiology Research in Higher Education
Content Type	Text
Resource Type	Article
Subject	Molecular Biology Microbiology

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