Mycobacterium smegmatis SftH exemplifies a distinctive clade of superfamily II DNA-dependent ATPases with 3' to 5' translocase and helicase activities Journal Article

   

Authors:	Yakovleva, L.; Shuman, S.
Article Title:	Mycobacterium smegmatis SftH exemplifies a distinctive clade of superfamily II DNA-dependent ATPases with 3' to 5' translocase and helicase activities
Abstract:	Bacterial DNA helicases are nucleic acid-dependent NTPases that play important roles in DNA replication, recombination and repair. We are interested in the DNA helicases of Mycobacteria, a genus of the phylum Actinobacteria, which includes the human pathogen Mycobacterium tuberculosis and its avirulent relative Mycobacterium smegmatis. Here, we identify and characterize M. smegmatis SftH, a superfamily II helicase with a distinctive domain structure, comprising an N-terminal NTPase domain and a C-terminal DUF1998 domain (containing a putative tetracysteine metal-binding motif). We show that SftH is a monomeric DNAdependent ATPase/dATPase that translocates 3' to 50 on single-stranded DNA and has 3' to 5' helicase activity. SftH homologs are found in bacteria representing 12 different phyla, being especially prevalent in Actinobacteria (including M. tuberculosis). SftH homologs are evident in more than 30 genera of Archaea. Among eukarya, SftH homologs are present in plants and fungi. © The Author(s) 2012.
Journal Title:	Nucleic Acids Research
Volume:	40
Issue:	15
ISSN:	0305-1048
Publisher:	Oxford University Press
Date Published:	2012-08-01
Start Page:	7465
End Page:	7475
Language:	English
DOI:	10.1093/nar/gks417
PROVIDER:	scopus
PMCID:	PMC3424565
PUBMED:	22641846
DOI/URL:	http://www.scopus.com/inward/record.url?eid=2-s2.0-84867287299&partnerID=40&md5=508bcb076dd18d3ab7a31e2962c39b66
Notes:	--- - "Export Date: 2 November 2012" - "CODEN: NARHA" - "Source: Scopus"

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