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5S rRNA binding ribosomal proteins from Thermus thermophilus : identification and some structural properties
Author(s) -
Gongadze G.,
Kashparov I.,
Lorenz S.,
Schroeder W.,
Erdmann V.A.,
Liljas A.,
Garber M.
Publication year - 1996
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(96)00457-7
Subject(s) - thermus thermophilus , ribosomal rna , ribosomal protein , identification (biology) , computational biology , thermus , 30s , chemistry , biology , biochemistry , ribosome , thermophile , rna , gene , enzyme , escherichia coli , botany
An unusual acidic ribosomal protein from Thermus thermophilus , TL5, that binds to 5S rRNA specifically and strongly, has been investigated. The N‐terminal sequence of TL5 does not reveal any homology with known ribosomal proteins. Two large tryptic fragments of TL5 have been isolated and characterized. 5S rRNA protected TL5 and its unstable N‐terminal fragment against trypsin action. The 5S rRNA binding ability of TL5 is probably inherent in its N‐terminal part. The other 5S rRNA binding ribosomal protein from T. thermophilus , TL4, has been identified as a homolog of the ribosomal protein L5 from Escherichia coli .