The primary structure of an acidic ribosomal protein from streptomyces griseus
| Autor: | Takuzi Itoh, Masanori Sugiyama, Ken-ichi Higo |
|---|---|
| Rok vydání: | 1982 |
| Předmět: |
chemistry.chemical_classification
Chymotrypsin Protease biology Edman degradation medicine.medical_treatment Biophysics Protein primary structure biology.organism_classification Biochemistry Amino acid chemistry Structural Biology Ribosomal protein biology.protein medicine Molecular Biology Streptomyces griseus Peptide sequence |
| Zdroj: | Biochimica et Biophysica Acta (BBA) - Protein Structure and Molecular Enzymology. 701:164-172 |
| ISSN: | 0167-4838 |
| DOI: | 10.1016/0167-4838(82)90109-1 |
| Popis: | The complete primary structure of a L7/L12-type acidic ribosomal protein (SA1) from actinomycetes or mycelial bacterium Streptomyces griseus has been determined. SA1 is composed of 125 amino acid residues and has the composition: Asp 7 , Thr 5 , Ser 5 , Glu 18 , Gln 4 , Pro 4 , Gly 8 , Ala 24 , Val 13 , Met 1 Ile 4 , Leu 12 , Phe 5 , Lys 14 and Arg 1 The molecular weight of SA1 is 13069. The amino acid sequence was determined by a combination of automated Edman degradation of the intact protein in a Beckman sequenator, and 4- N , N -dimethylaminoazobenzene-4′-isothiocyanate/phenylisothiocyanate double-coupling degradafion of the peptides obtained by digestions with trypsin, chymotrypsin, pepsin and Staphylococcus aureus protease of the intact protein. When the amino-terminal sequence of the SA1 (the first 39 residues) was compared to those of equivalent proteins from other eubacteria, the highest degree of similarity was found with that from Arthrobacter glacialis . The acidic ribosomal proteins from these two Gram-positive bacteria (S. griseus and A. glacialis) are somewhat distinct, in amino acid sequence and in amino acid compositions, from those of other Gram-negative and Gram-positive bacteria so far studied. However, they still appear to retain the characteristic prokaryotic-type structure. |
| Databáze: | OpenAIRE |
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