Primary structure of the hip gene of Escherichia coli and of its product, the β subunit of integration host factor

Flamm, Eric L.; Weisberg, Robert A.

doi:10.1016/0022-2836(85)90206-2

Cited by 161 publications

(65 citation statements)

References 30 publications

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“…IHF is composed of two nonidentical subunits, a and ,B, encoded by the himA (32) and hip (12) genes, respectively. IHF binds in the DNA minor groove (54) and imparts a bend to the DNA in excess of 1400 (27,36,38,49).…”

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HU and integration host factor function as auxiliary proteins in cleavage of phage lambda cohesive ends by terminase

1991

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HU and iategrtion host factor (IHF) are small, basic heterodimeric DNA-binding proteins which participate in transcripion Intatin, DNA replication, and recom . We constructed isogenic Escherichia coli stains in which fIU, THF, or both proteins were absent. Bacteriophage X did not grow in hosts lacing both HU and THE. Phage DNA replication and late gene transcription were normal in the double mutants, but packaging of A DNA was defective. Mature phage DNA molecules were absent, indicating that terminase was unable to linearize K DNA. Phage variants carrying a small substitution near cos or the ohml mutation in the terminase gene, Nul, formed plaques on HU-IHF-strains. We propose that HU or THU is required to establish the higher-order DNA-protein structure at cos that is the substrate for K terminase.DNA-protein complexes with a high degree of organization form at the initiation of DNA replication and are intermediates in several DNA recombination reactions. The ordered structures arise from the concerted assembly of a number of proteins on supercoiled DNA and bring nucleotide sequences located at a distance or on separate molecules into close proximity. In some of these reactions, the DNA bending required to form the complexes is facilitated by low-molecular-weight basic DNA-binding proteins (reviewed by Travers [50]).The best-studied Escherichia coli proteins of this type are the integration host factor (IHF) and HU (reviewed by Drlica and Rouviere-Yaniv [7] and Friedman [14]). IHF is composed of two nonidentical subunits, a and ,B, encoded by the himA (32) and hip (12) genes, respectively. IHF binds in the DNA minor groove (54) and imparts a bend to the DNA in excess of 1400 (27,36,38,49). The binding of IHF to specific DNA sequences at the K attachment site promotes A integration and excision. In a role that is probably related to DNA bending, IHF bound at K promoters can inhibit (22) (10). Although k packaging can take place in THF-hosts, an absolute requirement for IHF can be seen when the phage carries a cos site mutation (cosl54 or cos59) (1,31) or when the host canries a DNA gyrase mutation (15). Phage carrying the ohml mutation in the Nul gene will form plaques on IHF-gyrB hosts (21; also see reference 9).The genes coding for the a and ,B subunits of HU, hupA and hupB, respectively, have recently been cloned (25,26

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“…IHF and HU possess similar overall structures and share several regions of conserved homology (12,52). For certain reactions, the two proteins can act synergistically or interchangeably.…”

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HU and integration host factor function as auxiliary proteins in cleavage of phage lambda cohesive ends by terminase

1991

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“…The biological role of the structure observed after Mu infection of lysogens or minicells has been the subject of discussion (12,13,15,22,25 (3). This is expected, because himA and himD encode subunits of the same protein, integration host factor (11,20). If Mu lysogenization is influenced by integration host factor, then the phenotypes of himA and himD mutants should be similar.…”

Section: Resultsmentioning

confidence: 99%

Intermediates in bacteriophage Mu lysogenization of Escherichia coli him hosts

Bourret

Fox

1988

J Bacteriol

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Characterization of a putative intermediate in the Mu lysogenization pathway is possible in a variant Escherichia coli himD strain which exhibits greatly diminished lysogen formation. In this strain, most infecting Mu genomes form stable, transcribable, nonreplicating structures. Many of these genomes can be mobilized to form lysogens by a second Mu infection, which can be delayed by at least 100 min. This intermediate structure can be formed in the absence of Mu A or B function. We suggest that the inferred intermediate could be the previously reported protein-linked circular form of the Mu genome. Providing Mu B function from a plasmid enhances Mu lysogenization in this him strain, and the enhancement is much greater when both Mu A and B functions are provided.

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“…11,12) ECIHFa and ECIHF b are the a and b subunits of Escherichia coli IHF, respectively. 28,29) STHUa and STHU b are the a and b subunits of Salmonella thyphimurium HU, respectively. 30,31) BSHU and PAHU are Bacillus subtilis HU 32) and Psudomonas aeruginosa HU, 33) respectively.…”

Section: Cloning Of 23 Kb-dna Fragment Containing B Longum Hup Genementioning

confidence: 99%

Cloning and Expression inEscherichia coliof a Gene,hup, Encoding the Histone-like Protein HU ofBifidobacterium longum

Takeuchi

Matsumura

Kano

2002

Bioscience, Biotechnology, and Biochemistry

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Primary structure of the hip gene of Escherichia coli and of its product, the β subunit of integration host factor

Cited by 161 publications

References 30 publications

HU and integration host factor function as auxiliary proteins in cleavage of phage lambda cohesive ends by terminase

HU and integration host factor function as auxiliary proteins in cleavage of phage lambda cohesive ends by terminase

Intermediates in bacteriophage Mu lysogenization of Escherichia coli him hosts

Cloning and Expression inEscherichia coliof a Gene,hup, Encoding the Histone-like Protein HU ofBifidobacterium longum

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