Borrelia burgdorferi EbfC defines a newly-identified, widespread family of bacterial DNA-binding proteins

Sean P. Riley; Tomasz Bykowski; Anne E. Cooley; Logan H. Burns; Kelly Babb; Catherine A. Brissette; Amy Bowman; Matthew Rotondi; Clarke M. Miller; Edward Demoll; Kap Lim; Michael G. Fried; Brian Stevenson

doi:10.1093/nar/gkp027

Borrelia burgdorferi EbfC defines a newly-identified, widespread family of bacterial DNA-binding proteins

Sean P. Riley, Tomasz Bykowski, Anne E. Cooley, Logan H. Burns, Kelly Babb, Catherine A. Brissette, Amy Bowman, Matthew Rotondi, Clarke M. Miller, Edward Demoll, Kap Lim, Michael G. Fried, Brian Stevenson

Research output: Contribution to journal › Article › peer-review

36 Scopus citations

Abstract

The Lyme disease spirochete, Borrelia burgdorferi, encodes a novel type of DNA-binding protein named EbfC. Orthologs of EbfC are encoded by a wide range of bacterial species, so characterization of the borrelial protein has implications that span the eubacterial kingdom. The present work defines the DNA sequence required for high-affinity binding by EbfC to be the 4 bp broken palindrome GTnAC, where 'n' can be any nucleotide. Two high-affinity EbfC-binding sites are located immediately 5′ of B. burgdorferi erp transcriptional promoters, and binding of EbfC was found to alter the conformation of erp promoter DNA. Consensus EbfC-binding sites are abundantly distributed throughout the B. burgdorferi genome, occurring approximately once every 1 kb. These and other features of EbfC suggest that this small protein and its orthologs may represent a distinctive type of bacterial nucleoid-associated protein. EbfC was shown to bind DNA as a homodimer, and site-directed mutagenesis studies indicated that EbfC and its orthologs appear to bind DNA via a novel α-helical 'tweezer'-like structure.

Original language	English
Pages (from-to)	1973-1983
Number of pages	11
Journal	Nucleic Acids Research
Volume	37
Issue number	6
DOIs	https://doi.org/10.1093/nar/gkp027
State	Published - 2009

Bibliographical note

Funding Information:
US National Institutes of Health (grant R01-AI044254 to B.S. and R01-GM070662 to M.F.); National Institutes of Health Training Grant in Microbial Pathogenesis T32-AI49795 (to S.R.); University of Kentucky Graduate School Dissertation Year Fellowship (to S.R.). Funding for open access charge: US National Institutes of Health (grant R01-AI044254).

Funding

US National Institutes of Health (grant R01-AI044254 to B.S. and R01-GM070662 to M.F.); National Institutes of Health Training Grant in Microbial Pathogenesis T32-AI49795 (to S.R.); University of Kentucky Graduate School Dissertation Year Fellowship (to S.R.). Funding for open access charge: US National Institutes of Health (grant R01-AI044254).

Funders	Funder number
University of Kentucky Graduate School Dissertation Year Fellowship
National Institutes of Health (NIH)	R01-GM070662, R01-AI044254
National Institute of Allergy and Infectious Diseases	T32AI049795

ASJC Scopus subject areas

Genetics

Access to Document

10.1093/nar/gkp027

Cite this

@article{d16f6f32d71e48a5a517ee7c459dead2,

title = "Borrelia burgdorferi EbfC defines a newly-identified, widespread family of bacterial DNA-binding proteins",

abstract = "The Lyme disease spirochete, Borrelia burgdorferi, encodes a novel type of DNA-binding protein named EbfC. Orthologs of EbfC are encoded by a wide range of bacterial species, so characterization of the borrelial protein has implications that span the eubacterial kingdom. The present work defines the DNA sequence required for high-affinity binding by EbfC to be the 4 bp broken palindrome GTnAC, where 'n' can be any nucleotide. Two high-affinity EbfC-binding sites are located immediately 5′ of B. burgdorferi erp transcriptional promoters, and binding of EbfC was found to alter the conformation of erp promoter DNA. Consensus EbfC-binding sites are abundantly distributed throughout the B. burgdorferi genome, occurring approximately once every 1 kb. These and other features of EbfC suggest that this small protein and its orthologs may represent a distinctive type of bacterial nucleoid-associated protein. EbfC was shown to bind DNA as a homodimer, and site-directed mutagenesis studies indicated that EbfC and its orthologs appear to bind DNA via a novel α-helical 'tweezer'-like structure.",

author = "Riley, {Sean P.} and Tomasz Bykowski and Cooley, {Anne E.} and Burns, {Logan H.} and Kelly Babb and Brissette, {Catherine A.} and Amy Bowman and Matthew Rotondi and Miller, {Clarke M.} and Edward Demoll and Kap Lim and Fried, {Michael G.} and Brian Stevenson",

note = "Funding Information: US National Institutes of Health (grant R01-AI044254 to B.S. and R01-GM070662 to M.F.); National Institutes of Health Training Grant in Microbial Pathogenesis T32-AI49795 (to S.R.); University of Kentucky Graduate School Dissertation Year Fellowship (to S.R.). Funding for open access charge: US National Institutes of Health (grant R01-AI044254).",

year = "2009",

doi = "10.1093/nar/gkp027",

language = "English",

volume = "37",

pages = "1973--1983",

number = "6",

}

TY - JOUR

T1 - Borrelia burgdorferi EbfC defines a newly-identified, widespread family of bacterial DNA-binding proteins

AU - Riley, Sean P.

AU - Bykowski, Tomasz

AU - Cooley, Anne E.

AU - Burns, Logan H.

AU - Babb, Kelly

AU - Brissette, Catherine A.

AU - Bowman, Amy

AU - Rotondi, Matthew

AU - Miller, Clarke M.

AU - Demoll, Edward

AU - Lim, Kap

AU - Fried, Michael G.

AU - Stevenson, Brian

N1 - Funding Information: US National Institutes of Health (grant R01-AI044254 to B.S. and R01-GM070662 to M.F.); National Institutes of Health Training Grant in Microbial Pathogenesis T32-AI49795 (to S.R.); University of Kentucky Graduate School Dissertation Year Fellowship (to S.R.). Funding for open access charge: US National Institutes of Health (grant R01-AI044254).

PY - 2009

Y1 - 2009

N2 - The Lyme disease spirochete, Borrelia burgdorferi, encodes a novel type of DNA-binding protein named EbfC. Orthologs of EbfC are encoded by a wide range of bacterial species, so characterization of the borrelial protein has implications that span the eubacterial kingdom. The present work defines the DNA sequence required for high-affinity binding by EbfC to be the 4 bp broken palindrome GTnAC, where 'n' can be any nucleotide. Two high-affinity EbfC-binding sites are located immediately 5′ of B. burgdorferi erp transcriptional promoters, and binding of EbfC was found to alter the conformation of erp promoter DNA. Consensus EbfC-binding sites are abundantly distributed throughout the B. burgdorferi genome, occurring approximately once every 1 kb. These and other features of EbfC suggest that this small protein and its orthologs may represent a distinctive type of bacterial nucleoid-associated protein. EbfC was shown to bind DNA as a homodimer, and site-directed mutagenesis studies indicated that EbfC and its orthologs appear to bind DNA via a novel α-helical 'tweezer'-like structure.

AB - The Lyme disease spirochete, Borrelia burgdorferi, encodes a novel type of DNA-binding protein named EbfC. Orthologs of EbfC are encoded by a wide range of bacterial species, so characterization of the borrelial protein has implications that span the eubacterial kingdom. The present work defines the DNA sequence required for high-affinity binding by EbfC to be the 4 bp broken palindrome GTnAC, where 'n' can be any nucleotide. Two high-affinity EbfC-binding sites are located immediately 5′ of B. burgdorferi erp transcriptional promoters, and binding of EbfC was found to alter the conformation of erp promoter DNA. Consensus EbfC-binding sites are abundantly distributed throughout the B. burgdorferi genome, occurring approximately once every 1 kb. These and other features of EbfC suggest that this small protein and its orthologs may represent a distinctive type of bacterial nucleoid-associated protein. EbfC was shown to bind DNA as a homodimer, and site-directed mutagenesis studies indicated that EbfC and its orthologs appear to bind DNA via a novel α-helical 'tweezer'-like structure.

UR - http://www.scopus.com/inward/record.url?scp=64549106854&partnerID=8YFLogxK

UR - http://www.scopus.com/inward/citedby.url?scp=64549106854&partnerID=8YFLogxK

U2 - 10.1093/nar/gkp027

DO - 10.1093/nar/gkp027

M3 - Article

C2 - 19208644

AN - SCOPUS:64549106854

SN - 0305-1048

VL - 37

SP - 1973

EP - 1983

JO - Nucleic Acids Research

JF - Nucleic Acids Research

IS - 6

ER -

Borrelia burgdorferi EbfC defines a newly-identified, widespread family of bacterial DNA-binding proteins

Abstract

Bibliographical note

Funding

ASJC Scopus subject areas

Access to Document

Other files and links

Fingerprint

Cite this