A bacteriophage mimic of the bacterial nucleoid-associated protein Fis
Authors:
- S. Chakraborti,
- D. Balakrishnan,
- A.J. Trotter,
- W.H. Gittens,
- A.W.H. Yang,
- A. Jolma,
- J.R. Paterson,
- S. Swiatek,
- J. Plewka,
- F.A. Curtis,
- L.Y. Bowers,
- L.-O. Pålsson,
- T.R. Hughes,
- Michał Taube,
- Maciej Kozak,
- J.G. Heddle,
- G.J. Sharples
Abstract
We report the identification and characterization of a bacteriophage λ-encoded protein, NinH. Sequence homology suggests similarity between NinH and Fis, a bacterial nucleoid-associated protein (NAP) involved in numerous DNA topology manipulations, including chromosome condensation, transcriptional regulation and phage site-specific recombination. We find that NinH functions as a homodimer and is able to bind and bend double-stranded DNA in vitro. Furthermore, NinH shows a preference for a 15 bp signature sequence related to the degenerate consensus favored by Fis. Structural studies reinforced the proposed similarity to Fis and supported the identification of residues involved in DNA binding which were demonstrated experimentally. Overexpression of NinH proved toxic and this correlated with its capacity to associate with DNA. NinH is the first example of a phage-encoded Fis-like NAP that likely influences phage excision-integration reactions or bacterial gene expression. © 2020 The Author(s).
- Record ID
- UAM8c89fa14f0554ffb812ab8dd5b274202
- Author
- Journal series
- Biochemical Journal, ISSN 0264-6021, e-ISSN 1470-8728
- Issue year
- 2020
- Vol
- 477
- No
- 7
- Pages
- 1345-1362
- Publication size in sheets
- 0.90
- Keywords in English
- carrier proteins and binding proteins; curved DNA; dimer; double stranded DNA; Escherichia coli protein; factor for inversion stimulation; genomic DNA; homodimer; monomer; ninh protein; unclassified drug; virus DNA, amino terminal sequence; Article; bacterial cell; bacterial growth; bacteriophage; carboxy terminal sequence; chromosome condensation; computer model; consensus sequence; controlled study; crystal structure; dimerization; DNA binding; DNA metabolism; DNA structure; energy transfer; Escherichia coli; excision; gel mobility shift assay; gene expression; in vitro study; nonhuman; priority journal; protein analysis; protein conformation; protein purification; protein secondary structure; sedimentation rate; sequence alignment; sequence homology; structural homology; transcription regulation
- ASJC Classification
- ; ;
- DOI
- DOI:10.1042/BCJ20200146 Opening in a new tab
- URL
- https://www.scopus.com/inward/record.uri?eid=2-s2.0-85085659327&doi=10.1042%2fBCJ20200146&partnerID=40&md5=cf45dd952bedf2ce091a4ca2a69092b6 Opening in a new tab
- Language
- (en) English
- Score (nominal)
- 100
- Score source
- journalList
- Score
- = 100.0, 14-05-2022, ArticleFromJournal
- Publication indicators
- = 0; : 2018 = 1.078; : 2019 (2 years) = 4.097 - 2019 (5 years) =4.086
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- Uniform Resource Identifier
- https://researchportal.amu.edu.pl/info/article/UAM8c89fa14f0554ffb812ab8dd5b274202/
- URN
urn:amu-prod:UAM8c89fa14f0554ffb812ab8dd5b274202
* presented citation count is obtained through Internet information analysis and it is close to the number calculated by the Publish or PerishOpening in a new tab system.