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The carboxyl extension of a ubiquitin-like protein is rat ribosomal protein S30.
- Source :
-
The Journal of biological chemistry [J Biol Chem] 1993 Aug 25; Vol. 268 (24), pp. 17967-74. - Publication Year :
- 1993
-
Abstract
- The amino acid sequence of the rat 40 S ribosomal subunit protein S30 was deduced from the sequence of nucleotides in a recombinant cDNA and confirmed by the determination of the 18 residues at the NH2 terminus of the protein. Unlike the majority of ribosomal proteins, which are unprocessed primary products of the translation of their mRNAs, S30 is formed by cleavage from a larger hybrid protein. The NH2-terminal polypeptide has 38% identity with ubiquitin and contains the characteristic carboxyl-terminal Gly-Gly dipeptide of this family of proteins. S30 has 59 amino acids and the molecular weight is 6,643; the ubiquitin-like sequence has 74 residues and the molecular weight is 7,634. The hybrid protein is encoded in each of the 8-10 members of the family of rat S30 genes; there is, however, only a single species of mRNA which contains the sequences for both proteins. The coding sequence of the hybrid protein occurs in the reverse polarity in the genome of the Finkel-Biskis-Reilly murine sarcoma virus.
- Subjects :
- Amino Acid Sequence
Animals
Base Sequence
DNA
Molecular Sequence Data
Molecular Weight
Oligodeoxyribonucleotides
Open Reading Frames
Protein Biosynthesis
RNA, Messenger biosynthesis
Rats
Recombinant Fusion Proteins chemistry
Recombinant Proteins chemistry
Ribosomal Proteins chemistry
Sequence Homology, Amino Acid
Sequence Homology, Nucleic Acid
Transcription, Genetic
Ubiquitins chemistry
RNA, Messenger metabolism
Ribosomal Proteins genetics
Ubiquitins genetics
Subjects
Details
- Language :
- English
- ISSN :
- 0021-9258
- Volume :
- 268
- Issue :
- 24
- Database :
- MEDLINE
- Journal :
- The Journal of biological chemistry
- Publication Type :
- Academic Journal
- Accession number :
- 8394356