The primary structure of the DNA‐binding protein II from Clostridium pasteurianum
- 1 October 1984
- journal article
- research article
- Published by Wiley in FEBS Letters
- Vol. 175 (2), 208-212
- https://doi.org/10.1016/0014-5793(84)80738-3
Abstract
The complete amino acid sequence of the Clostridium pasteurianum DNA-binding protein II (DNAb-II) has been determined. The molecule contains 91 amino acid residues and has an M rof 10133. Sequence data were obtained from manual Edman degradation, using the DABITC/PITC double-coupling of the tryptic, peptic, chymotryptic and Staphylococcus protease peptides. A comparison of the amino acid sequence of the C. pasteurianum DNAb-II with those of the DNAb-II from Escherichia coli, Bacillus stearothermophilus, Thermoplasma acidophilum and Pseudomonas aeruginosa shows that the C. pasteurianum protein is more homologous to that of B. stearothermophilus (60%) than to that of E. coli (45%). All DNAb-II proteins have identical sequences Gly-Phe-Gly-X-Phe at positions 46–50 and Arg-Asn-Pro-X-Thr at positions 61–65.Keywords
This publication has 8 references indexed in Scilit:
- On the DNA binding protein II from Bacillus stearothermophilus. II. The amino acid sequence and its relation to those of homologous proteins from other prokaryotes.Journal of Biological Chemistry, 1983
- On the DNA binding protein II from Bacillus stearothermophilus. I. Purification, studies in solution, and crystallization.Journal of Biological Chemistry, 1983
- A single DNA‐binding protein from Pseudomonas aeruginosa homologous to proteins NS1 and NS2 (HU proteins) of Escherichia coli and other bacteriaFEBS Letters, 1981
- Proteins Controlling the Helical Structure of DNAAnnual Review of Biochemistry, 1981
- A histone-like protein (HTa) from Thermoplasma acidophilum. I. Purification and properties.Journal of Biological Chemistry, 1981
- A histone-like protein (HTa) from Thermoplasma acidophilum. II. Complete amino acid sequence.Journal of Biological Chemistry, 1981
- Primary structures of two homologous ribosome‐associated DNA‐binding proteins of Escherichia coliFEBS Letters, 1978
- Specific association of two homologous DNA-binding proteins to the native 30-S ribosomal subunits of Escherichia coliBiochimica et Biophysica Acta (BBA) - Nucleic Acids and Protein Synthesis, 1978