The primary structure of DNA binding protein II from the extreme thermophilic bacterium Thermus thermophilus

The primary structure of DNA binding protein II (DNA bp II) from the extreme thermophilic bacterium Thermus thermophilus has been established by combination of manual and automated techniques. The protein has 95 residues and a molecular mass of 11843. Comparison of the primary structure with the kno...

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Bibliographic Details
Published in:FEBS letters 1990-10, Vol.273 (1-2), p.59-62
Main Authors: Zierer, Rainer, Choli, Dora
Format: Article
Language:English
Subjects:
Amino Acid Sequence
Analytical, structural and metabolic biochemistry
Bacteria - metabolism
Bacterial Proteins
Biological and medical sciences
DNA-binding protein II
DNA-Binding Proteins - chemistry
DNA-Binding Proteins - genetics
Fundamental and applied biological sciences. Psychology
Homology
Molecular Sequence Data
molecular weight
Primary structure
Proteins
Sequence Homology, Nucleic Acid
Thermophilic bacteria
Thermus - metabolism
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Summary:The primary structure of DNA binding protein II (DNA bp II) from the extreme thermophilic bacterium Thermus thermophilus has been established by combination of manual and automated techniques. The protein has 95 residues and a molecular mass of 11843. Comparison of the primary structure with the known sequence data of DNA bp II from Clostridium pasteurineum, Baccillus stearothermophilus, Escherichia coli, Rhizobium meliloti, Anabena, Thermoplasma acidophilum, Pseudomonas aeruginosa and Bacillus caldolyticus reveals a clear homology among these small basic proteins. In particular, two short sequences in the middle and C-terminal part of the proteins (residues N-Gly-Phe-Gly-X-Phe and Pro-X-Thr at positions 46–51 and 63–65, respectively) are completely conserved.
ISSN:0014-5793
1873-3468
DOI:10.1016/0014-5793(90)81050-X