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J. Biol. Chem., Vol. 276, Issue 20, 16641-16648, May 18, 2001

This Article Full Text Full Text (PDF) All Versions of this Article: 276/20/16641    most recent M011295200v1 Submit a Letter to Editor Alert me when this article is cited Alert me when eLetters are posted Alert me if a correction is posted Citation Map Services Email this article to a friend Similar articles in this journal Similar articles in PubMed Alert me to new issues of the journal Download to citation manager Request Permissions Citing Articles Citing Articles via HighWire Citing Articles via Google Scholar Google Scholar Articles by Bartels, F. Articles by de Lorenzo, V. Search for Related Content PubMed PubMed Citation Articles by Bartels, F. Articles by de Lorenzo, V. Social Bookmarking                      What's this?

The Essential HupB and HupN Proteins of Pseudomonas putida Provide Redundant and Nonspecific DNA-bending Functions^*

Frank Bartels^§, Silvia Fernández^¶, Andreas Holtel, Kenneth N. Timmis, and Víctor de Lorenzo^¶**

From the  Division of Microbiology, Gesellschaft für Biotechnologische Forschung (GBF), D-38124, Braunschweig, Germany and ^¶ Department of Microbial Biotechnology, Centro Nacional de Biotecnología, Consejo Superior de Investigaciones Científicas, (CSIC), Campus de Cantoblanco, 28049 Madrid, Spain

A protein mixture containing two major components able to catalyze a -recombination reaction requiring nonspecific DNA bending was obtained by fractionation of a Pseudomonas putida extract. N-terminal sequence analysis and genomic data base searches identified the major component as an analogue of HupB of Pseudomonas aeruginosa and Escherichia coli, encoding one HU protein variant. The minor component of the fraction, termed HupN, was divergent enough from HupB to predict a separate DNA-bending competence. The determinants of the two proteins were cloned and hyperexpressed, and the gene products were purified. Their activities were examined in vitro in -recombination assays and in vivo by complementation of the Hbsu function of Bacillus subtilis. HupB and HupN were equally efficient in all tests, suggesting that they are independent and functionally redundant DNA bending proteins. This was reflected in the maintenance of in vivo activity of the ⁵⁴ Ps promoter of the toluene degradation plasmid, TOL, which requires facilitated DNA bending, in hupB or hupN strains. However, hupB/hupN double mutants were not viable. It is suggested that the requirement for protein-facilitated DNA bending is met in P. putida by two independent proteins that ensure an adequate supply of an essential cellular activity.

The nucleotide sequence(s) reported in this paper has been submitted to the GenBank^TM/EMBL Data Bank with accession number(s) AF345628 (hupB of P. putida); AF345629 (hupN of P. putida), and AF345630 (hupN of P. aeruginosa).

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