Zobrazeno 1 - 10
of 12
pro vyhledávání: '"Alicia M Chenail"'
Autor:
Brandon L Jutras, Alicia M Chenail, Christi L Rowland, Dustin Carroll, M Clarke Miller, Tomasz Bykowski, Brian Stevenson
Publikováno v:
PLoS ONE, Vol 8, Iss 6, p e66683 (2013)
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 bact
Externí odkaz:
https://doaj.org/article/188876b7980146c2be7d099babd2685e
Publikováno v:
Journal of Bacteriology. 199
Autor:
Brandon L. Jutras, Logan H. Burns, Amy Bowman, Ashutosh Verma, Brian Stevenson, Alicia M. Chenail, Claire A. Adams
Publikováno v:
Journal of Bacteriology. 199
The Borrelia burgdorferi BpaB proteins of the spirochete's ubiquitous cp32 prophages are DNA-binding proteins, required both for maintenance of the bacteriophage episomes and for transcriptional regulation of the cp32 erp operons. Through use of DNas
Autor:
Alicia M. Chenail, Ashutosh Verma, Alyssa D. Antonicello, Grant S. Jones, Brian Stevenson, Nicholas A. Brown, Brandon L. Jutras
Publikováno v:
Journal of Bacteriology. 195:4915-4923
Bacteria require explicit control over their proteomes in order to compete and survive in dynamic environments. The Lyme disease spirocheteBorrelia burgdorferiundergoes substantial protein profile changes during its cycling between vector ticks and v
Autor:
Brian Stevenson, Amy Bowman, Brandon L. Jutras, Dustin Carroll, Alicia M. Chenail, M. Clarke Miller, Haining Zhu
Publikováno v:
Journal of Biological Chemistry. 288:26220-26234
The PUR domain is a nucleic acid-binding motif found in critical regulatory proteins of higher eukaryotes and in certain species of bacteria. During investigations into mechanisms by which the Lyme disease spirochete controls synthesis of its Erp sur
Autor:
Claire A. Adams, Catherine A. Brissette, Brandon L. Jutras, Amy Bowman, Ashutosh Verma, Alicia M. Chenail, Brian Stevenson
Publikováno v:
Journal of Bacteriology. 194:3395-3406
Nearly every known species of Eubacteria encodes a homolog of the Borrelia burgdorferi EbfC DNA-binding protein. We now demonstrate that fluorescently tagged EbfC associates with B. burgdorferi nucleoids in vivo and that chromatin immunoprecipitation
Autor:
Brian Stevenson, Ashutosh Verma, Claire A. Adams, Amy Bowman, Brandon L. Jutras, Alicia M. Chenail, Logan H. Burns
Publikováno v:
Journal of Bacteriology. 194:4570-4578
The Borrelia burgdorferi BpaB proteins of the spirochete's ubiquitous cp32 prophages are DNA-binding proteins, required both for maintenance of the bacteriophage episomes and for transcriptional regulation of the cp32 erp operons. Through use of DNas
Autor:
Claire A. Adams, Amy Bowman, Sean P. Riley, Michael Fried, Alicia M. Chenail, Brandon L. Jutras, Logan H. Burns, Kelly Babb, Anne E. Cooley, Alisha M Moore, Laura A. Haselhorst, Brian Stevenson
Publikováno v:
Nucleic Acids Research
Borrelia burgdorferi produces Erp outer surface proteins throughout mammalian infection, but represses their synthesis during colonization of vector ticks. A DNA region 50 of the start of erp transcription, Operator 2, was previously shown to be esse
Autor:
Brandon L, Jutras, Alicia M, Chenail, Dustin W, Carroll, M Clarke, Miller, Haining, Zhu, Amy, Bowman, Brian, Stevenson
Publikováno v:
The Journal of Biological Chemistry
Background: Borrelia burgdorferi controls protein production during its infectious cycle. Results: Bpur was identified and shown to enhance effects of the erp transcriptional repressor, BpaB. Details of Bpur-nucleic acid interactions were obtained. C
Publikováno v:
Journal of bacteriology. 195(4)
The Lyme disease spirochete controls production of its OspC and Erp outer surface proteins, repressing protein synthesis during colonization of vector ticks but increasing expression when those ticks feed on vertebrate hosts. Early studies found that