Literature DB >> 8609614

Histone-like protein HU and bacterial DNA topology: suppression of an HU deficiency by gyrase mutations.

M Malik1, A Bensaid, J Rouviere-Yaniv, K Drlica.   

Abstract

The abundant bacterial protein called HU has the ability to wrap and bend DNA in vitro, and thus it has long been thought to play a role in DNA supercoiling. In the absence of HU, Escherichia coli formed tiny colonies on agar, rapidly accumulated suppressor mutations, and was hypersensitive to novobiocin. Three types of evidence implicated gyrase in the suppression of an HU deficiency. First, spontaneous suppressors that restored normal growth and reduced sensitivity to novobiocin mapped in gyrB, one of the genes encoding DNA gyrase. Second, a pair of known gyrB mutations (gyrB-203 Ts gyrB-221 NovR) allowed normal growth at permissive (30 degrees C) but not at intermediate (37 degrees C) conditions. Third, introduction of a gyrB-expressing plasmid restored normal colony size. DNA supercoiling comparisons showed that chromosomal supercoiling decreased in the absence of HU and increased toward wild-type levels in the presence of a spontaneous gyrB suppressor. Taken together, these data establish that HU has a physiological role in chromosomal DNA topology, probably by facilitating the action of gyrase.

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Year:  1996        PMID: 8609614     DOI: 10.1006/jmbi.1996.0068

Source DB:  PubMed          Journal:  J Mol Biol        ISSN: 0022-2836            Impact factor:   5.469


  35 in total

1.  The histone-like protein HU does not obstruct movement of T7 RNA polymerase in Escherichia coli cells but stimulates its activity.

Authors:  Pilar Morales; Josette Rouviere-Yaniv; Marc Dreyfus
Journal:  J Bacteriol       Date:  2002-03       Impact factor: 3.490

2.  A functional assay in Escherichia coli to detect non-assisted interaction between galactose repressor dimers.

Authors:  N Perez; M Rehault; M Amouyal
Journal:  Nucleic Acids Res       Date:  2000-09-15       Impact factor: 16.971

3.  Impact of gyrA and parC mutations on quinolone resistance, doubling time, and supercoiling degree of Escherichia coli.

Authors:  S Bagel; V Hüllen; B Wiedemann; P Heisig
Journal:  Antimicrob Agents Chemother       Date:  1999-04       Impact factor: 5.191

4.  Spiral structure of Escherichia coli HUalphabeta provides foundation for DNA supercoiling.

Authors:  Fusheng Guo; Sankar Adhya
Journal:  Proc Natl Acad Sci U S A       Date:  2007-03-05       Impact factor: 11.205

5.  Coordination of genomic structure and transcription by the main bacterial nucleoid-associated protein HU.

Authors:  Michael Berger; Anca Farcas; Marcel Geertz; Petya Zhelyazkova; Klaudia Brix; Andrew Travers; Georgi Muskhelishvili
Journal:  EMBO Rep       Date:  2009-11-13       Impact factor: 8.807

6.  In vitro DNA binding of the archaeal protein Sso7d induces negative supercoiling at temperatures typical for thermophilic growth.

Authors:  P López-García; S Knapp; R Ladenstein; P Forterre
Journal:  Nucleic Acids Res       Date:  1998-05-15       Impact factor: 16.971

7.  The Escherichia coli histone-like protein HU affects DNA initiation, chromosome partitioning via MukB, and cell division via MinCDE.

Authors:  A Jaffe; D Vinella; R D'Ari
Journal:  J Bacteriol       Date:  1997-06       Impact factor: 3.490

Review 8.  DNA gyrase, topoisomerase IV, and the 4-quinolones.

Authors:  K Drlica; X Zhao
Journal:  Microbiol Mol Biol Rev       Date:  1997-09       Impact factor: 11.056

Review 9.  Architectural organization in E. coli nucleoid.

Authors:  Mirjana Macvanin; Sankar Adhya
Journal:  Biochim Biophys Acta       Date:  2012-02-22

10.  Escherichia coli strains lacking protein HU are UV sensitive due to a role for HU in homologous recombination.

Authors:  S Li; R Waters
Journal:  J Bacteriol       Date:  1998-08       Impact factor: 3.490

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