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The complete amino acid sequence of the ribosomal A protein (L12) from the archaebacterium Sulfolobus acidocaldarius
Author(s) -
Matheson A.T.,
Louie K.A.,
Böck August
Publication year - 1988
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(88)80844-5
Subject(s) - sulfolobus acidocaldarius , sulfolobus , ribosomal protein , biochemistry , peptide sequence , amino acid , lysine , biology , 30s , protein sequencing , homology (biology) , ribosomal rna , sequence (biology) , archaea , ribosome , gene , rna
The ribosomal A protein (SacL12) from the archaebacterium Sulfolobus acidocaldarius has been sequenced. The protein contains 105 amio acids, has a composition of Asp 2 , Asn 3 , Thr 4 , Ser 6 , Glu 17 , Gln 4 , Pro 3 , Gly 7 , Ala 18 , Val 7 , Met 2 , Ile 7 , Leu 9 , Tyr 2 , Phe 1 , His 1 , Lys 11 , Arg 1 , and a molecular mass of 11 126 Da. The Sulfolobus protein shows many features in common with the equivalent proteins in the eukaryotes such as 35–40% sequence homology and similar hydrophilicity profiles, features much less evident when this protein is compared to eubacterial L12 proteins. SacL12 contains an unusual sequence of alternating clusters of lysine and glutamic acid (—EKKEEKKEEEKK—) in the C‐terminal region. Similar sequences are found in some eukaryotic L12 proteins.