Primary structures of two homologous ribosome‐associated DNA‐binding proteins of <i>Escherichia coli</i>

Mende, Liane; Timm, Beate; Subramanian, Alap R.

doi:10.1016/0014-5793(78)80446-3

Cited by 86 publications

(18 citation statements)

References 11 publications

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“…Following the addition of carboxypeptidase A, 0.3 mol alanine, 0.5 mol valine and 0.5 mol lysine/mol protein were released after a l-h digestion. The position of peptide T-13 (residues 84 -86) assigned by difference is the only one which fits with the carboxy-terminal sequence of peptide Our results are in complete agreement with those obtained with a different strategy by Mende et al [8] AC-3. who have determined the primary structure of proteins NS-1 and NS-2 from E. coli (strains MRE 600 and CP 78).…”

Section: Complete Sequence Of Proteins Hu-1 and Hu-2supporting

confidence: 91%

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Complete Amino‐Acid Sequences of DNA‐Binding Proteins HU‐1 and HU‐2 from Escherichia coli

Lainé

Kmiecik

Sáutière

et al. 1980

European Journal of Biochemistry

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The DNA-binding protein HU from Escherichia coli is a heterodimer constituted of two polypeptide chains termed HU-1 and HU-2, of 90 residues each. Their primary structures were established from structural data obtained from tryptic peptides of each monomer in addition to the structural data provided by the automated Edman degradation of the dimer and by peptides derived from cleavage of the dimer with trypsin, chymotrypsin, V8 staphylococcal protease and dilute acid. The results presented in this paper confirm the amino-terminal and carboxy-terminal sequences of the dimer HU reported previously ) FEBS Lett. 89, 116-1201. The amino acid sequences of proteins HU-1 and HU-2 are identical to those of proteins NS-1 and NS-2 respectivcly, determined independently by Mende et al. [FEBS Lett. (1978) 96, 395-3981.The amino acid sequences of proteins HU-1 and HU-2 are closely related but differ by 28 residues. These proteins are characterized by their high content of hydrophobic residues represented mostly by alanine. In both proteins, half of the basic residues are scattered along the polypeptide chain and the remainder is found within two short sequences located in the carboxyterminal part of the molecule.No sequence homology could be established between the proteins HU-1 and HU-2 and any one of the five histones from different eukaryotes.

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Section: Complete Sequence Of Proteins Hu-1 and Hu-2supporting

confidence: 91%

“…Thus, the structural data obtained from the dimer together with those obtained from HU-1 and HU-2 allowed us to determine the complete amino acid sequences of proteins HU-1 and HU-2. Our results are in complete agreement with those obtained independently by Mende et al [8] with a different strategy.…”

supporting

confidence: 94%

Complete Amino‐Acid Sequences of DNA‐Binding Proteins HU‐1 and HU‐2 from Escherichia coli

Lainé

Kmiecik

Sáutière

et al. 1980

European Journal of Biochemistry

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“…The hbs gene is located on a 900-bp EcoRI-NdeI chromosomal fragment. In E. coli and Salmonella typhimurium, two genes were found to encode closely related proteins (HU2 and HU1) that form the heterodimeric protein HU (17,25,26,(30)(31)(32). The availability of the genes encoding HU in E. coli and S. typhimurium facilitated studies of its biological role in vivo.…”

Section: Dna-binding Protein Of B Subtilis 3197mentioning

confidence: 99%

“…The best-studied and most abundant protein is HU, present in Escherichia coli. It exists predominantly as a heterodimer (HU2 and HU1) encoded by the genes hupA and hupB (25,26,30,32). The two subunits consist of 90 amino acid residues each and have 70% identical residues.…”

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confidence: 99%

Molecular cloning, nucleotide sequence, and characterization of the Bacillus subtilis gene encoding the DNA-binding protein HBsu

et al. 1991

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A homologous class of histonelike proteins which are believed to wrap the DNA and to condense the chromosome into highly folded nucleoid structures has been identified in different bacterial species. Bacillus subtilis encodes a homodimeric DNA-binding protein called HBsu. We have cloned the corresponding gene (hbs) on a 3.8-kb fragment. The gene was subcloned to a 1-kb fragment, sequenced, and characterized. It encodes a 92-amino-acid protein with a predicted molecular mass of 9,884 Da. Fortunately, analysis of the DNA sequence downstream of the 3' end of hbs revealed the location of the first 19 amino acid residues of MtrA. This finding located the hbs gene unequivocally to the 5' end of the mtr operon at about 2040 on the standard genetic map of B. subtilis. Northern (RNA) blot analysis and primer extension studies indicated the presence of two distinct hbs transcripts, which were found to be initiated at two different sites located about 160 bases apart. Several attempts to replace the hbs gene in the B. subtilis chromosome with a cat-interrupted copy (hbs::cat) through marker replacement recombination were unsuccessful. In order to study whether hbs is an essential gene, we have constructed a strain containing a truncated copy of the gene behind its own promoter and another intact copy under control of the isopropyl-,-D-thiogalactopyranoside (IPTG)-inducible spac-1 promoter. In this strain (BM19), normal growth was found to depend on IPTG, whereas in the absence of IPTG, growth was severely affected. These results suggest an essential role for the hbs gene product for normal growth in B. subtilis.

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“…Protein HTa condenses linear double-stranded DNA into globular particles [19]. The proteins HU-1 and HU-2 [8,9] and the protein HTa [20] have been completely sequenced. The partial sequences of the HU-type proteins from P. aeruginoscr [I I] and from the Cyanobacterium Syneclzocvstis 1211 have also been reported.…”

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confidence: 99%

Primary Structure of the DNA-Binding Protein HRm from Rhizobium meliloti

et al. 1983

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The amino acid sequence of protein HRm, a DNA‐binding HU‐type protein of 90 residues (Mr 9303), isolated from Rhizobium meliloti, has been established from automated sequence analysis of the protein and from structural data provided by peptides derived from cleavage of the protein at arginine and aspartic acid residues. The comparison of the primary structure of protein HRm with that of other HU‐type proteins shows that two short sequences, of 7 and 6 residues respectively, located in the median part of the molecule, appear highly conserved and may be important in the function of the protein.

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Primary structures of two homologous ribosome‐associated DNA‐binding proteins of Escherichia coli

Cited by 86 publications

References 11 publications

Complete Amino‐Acid Sequences of DNA‐Binding Proteins HU‐1 and HU‐2 from Escherichia coli

Complete Amino‐Acid Sequences of DNA‐Binding Proteins HU‐1 and HU‐2 from Escherichia coli

Molecular cloning, nucleotide sequence, and characterization of the Bacillus subtilis gene encoding the DNA-binding protein HBsu

Primary Structure of the DNA-Binding Protein HRm from Rhizobium meliloti

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