Eubacterial SpoVG homologs constitute a new family of site-specific DNA-binding proteins.

A site-specific DNA-binding protein was purified from Borrelia burgdorferi cytoplasmic extracts, and determined to be a member of the highly conserved SpoVG family. This is the first time a function has been attributed to any of these ubiquitous bacterial proteins. Further investigations into SpoVG...

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Autores principales:	Brandon L Jutras, Alicia M Chenail, Christi L Rowland, Dustin Carroll, M Clarke Miller, Tomasz Bykowski, Brian Stevenson
Formato:	article
Lenguaje:	EN
Publicado:	Public Library of Science (PLoS) 2013
Materias:	Medicine R Science Q
Acceso en línea:	https://doaj.org/article/188876b7980146c2be7d099babd2685e
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spelling	oai:doaj.org-article:188876b7980146c2be7d099babd2685e2021-11-18T07:40:57ZEubacterial SpoVG homologs constitute a new family of site-specific DNA-binding proteins.1932-620310.1371/journal.pone.0066683https://doaj.org/article/188876b7980146c2be7d099babd2685e2013-01-01T00:00:00Zhttps://www.ncbi.nlm.nih.gov/pmc/articles/pmid/23818957/?tool=EBIhttps://doaj.org/toc/1932-6203A site-specific DNA-binding protein was purified from Borrelia burgdorferi cytoplasmic extracts, and determined to be a member of the highly conserved SpoVG family. This is the first time a function has been attributed to any of these ubiquitous bacterial proteins. Further investigations into SpoVG orthologues indicated that the Staphylococcus aureus protein also binds DNA, but interacts preferentially with a distinct nucleic acid sequence. Site-directed mutagenesis and domain swapping between the S. aureus and B. burgdorferi proteins identified that a 6-residue stretch of the SpoVG α-helix contributes to DNA sequence specificity. Two additional, highly conserved amino acid residues on an adjacent β-sheet are essential for DNA-binding, apparently by contacts with the DNA phosphate backbone. Results of these studies thus identified a novel family of bacterial DNA-binding proteins, developed a model of SpoVG-DNA interactions, and provide direction for future functional studies on these wide-spread proteins.Brandon L JutrasAlicia M ChenailChristi L RowlandDustin CarrollM Clarke MillerTomasz BykowskiBrian StevensonPublic Library of Science (PLoS)articleMedicineRScienceQENPLoS ONE, Vol 8, Iss 6, p e66683 (2013)
institution	DOAJ
collection	DOAJ
language	EN
topic	Medicine R Science Q
spellingShingle	Medicine R Science Q Brandon L Jutras Alicia M Chenail Christi L Rowland Dustin Carroll M Clarke Miller Tomasz Bykowski Brian Stevenson Eubacterial SpoVG homologs constitute a new family of site-specific DNA-binding proteins.
description	A site-specific DNA-binding protein was purified from Borrelia burgdorferi cytoplasmic extracts, and determined to be a member of the highly conserved SpoVG family. This is the first time a function has been attributed to any of these ubiquitous bacterial proteins. Further investigations into SpoVG orthologues indicated that the Staphylococcus aureus protein also binds DNA, but interacts preferentially with a distinct nucleic acid sequence. Site-directed mutagenesis and domain swapping between the S. aureus and B. burgdorferi proteins identified that a 6-residue stretch of the SpoVG α-helix contributes to DNA sequence specificity. Two additional, highly conserved amino acid residues on an adjacent β-sheet are essential for DNA-binding, apparently by contacts with the DNA phosphate backbone. Results of these studies thus identified a novel family of bacterial DNA-binding proteins, developed a model of SpoVG-DNA interactions, and provide direction for future functional studies on these wide-spread proteins.
format	article
author	Brandon L Jutras Alicia M Chenail Christi L Rowland Dustin Carroll M Clarke Miller Tomasz Bykowski Brian Stevenson
author_facet	Brandon L Jutras Alicia M Chenail Christi L Rowland Dustin Carroll M Clarke Miller Tomasz Bykowski Brian Stevenson
author_sort	Brandon L Jutras
title	Eubacterial SpoVG homologs constitute a new family of site-specific DNA-binding proteins.
title_short	Eubacterial SpoVG homologs constitute a new family of site-specific DNA-binding proteins.
title_full	Eubacterial SpoVG homologs constitute a new family of site-specific DNA-binding proteins.
title_fullStr	Eubacterial SpoVG homologs constitute a new family of site-specific DNA-binding proteins.
title_full_unstemmed	Eubacterial SpoVG homologs constitute a new family of site-specific DNA-binding proteins.
title_sort	eubacterial spovg homologs constitute a new family of site-specific dna-binding proteins.
publisher	Public Library of Science (PLoS)
publishDate	2013
url	https://doaj.org/article/188876b7980146c2be7d099babd2685e
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Eubacterial SpoVG homologs constitute a new family of site-specific DNA-binding proteins.

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