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Structural domains of ribosomal protein S8 and their relationship to ribosomal RNA binding
Author(s) -
Paterakis Konstantinos,
Littlechild Jennifer
Publication year - 1982
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/0014-5793(82)81125-3
Subject(s) - ribosomal rna , ribosomal protein , 5.8s ribosomal rna , 50s , biochemistry , 30s , chymotrypsin , cleavage (geology) , 23s ribosomal rna , trypsin , rna , ribosome , 5s ribosomal rna , microbiology and biotechnology , biology , chemistry , 18s ribosomal rna , enzyme , gene , paleontology , fracture (geology)
Escherichia coli ribosomal protein S8 has been subjected to mild proteolytic digestion in order to search for structural domains within the protein [1]. A characteristic fragment produced in high yield after chymotrypsin treatment has been located with the protein sequence. Circular dichroism has shown this domain to be rich in α helix. However, the fragment loses its ability to bind to 16 S rRNA as does a similar fragment produced by trypsin cleavage. The intact protein is required for rRNA binding and is highly protected against proteolytic digestion when bound to the RNA.