Proteolysis of ribosomal protein S1 from Escherichia coli and Thermus thermophilus leads to formation of two different fragments

As a result of limited tryptic proteolysis of S1 ribosomal protein (molecular mass 60 kD) from Thermus thermophilus, 25 N-terminal amino acid residues and 71 C-terminal amino acid residues are split off and a stable high-molecular-weight fragment with molecular mass of 49 kD is formed that retains R...

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Bibliographic Details
Published in:	Biochemistry (Moscow) Vol. 72; no. 11; pp. 1225 - 1232
Main Authors:	Selivanova, O M, Fedorova, Yu Yu, Serduyk, I N
Format:	Journal Article
Language:	English
Published:	United States Springer Nature B.V 01-11-2007
Subjects:	Amino Acid Sequence Amino acids Bacteria Bacterial Proteins - chemistry Bacterial Proteins - genetics Bacterial Proteins - isolation & purification E coli Escherichia coli Escherichia coli - chemistry Escherichia coli - genetics Escherichia coli Proteins - chemistry Escherichia coli Proteins - genetics Escherichia coli Proteins - isolation & purification Molecular Sequence Data Peptide Fragments - chemistry Peptide Fragments - genetics Peptide Fragments - isolation & purification Protein Binding Proteins Ribosomal Proteins - chemistry Ribosomal Proteins - genetics Ribosomal Proteins - isolation & purification Ribosomes - metabolism RNA, Bacterial - metabolism Thermus thermophilus Thermus thermophilus - chemistry Thermus thermophilus - genetics Trypsin
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Summary:	As a result of limited tryptic proteolysis of S1 ribosomal protein (molecular mass 60 kD) from Thermus thermophilus, 25 N-terminal amino acid residues and 71 C-terminal amino acid residues are split off and a stable high-molecular-weight fragment with molecular mass of 49 kD is formed that retains RNA-binding properties and is capable of interacting with 30S ribosomal subunit. Earlier, application of a similar procedure for the formation of a fragment of S1 protein from Escherichia coli resulted in splitting of 171 N-terminal amino acid residues with the formation of a 41.3 kD fragment that possesses RNA-binding properties only. Thus, in spite of high homology between E. coli and T. thermophilus proteins, the proteolysis leads to the formation of two different fragments, which points, in our opinion, to the fact of significant differences between their structures.
Bibliography:	ObjectType-Article-1 SourceType-Scholarly Journals-1 ObjectType-Feature-2 content type line 23
ISSN:	0006-2979 1608-3040 0320-9725
DOI:	10.1134/S0006297907110089