Methionine or not methionine at the beginning of a protein

BioEssays - Tập 3 Số 1 - Trang 27-31 - 1985
Fred Sherman1, John Stewart2, Susumu Tsunasawa3
1Department of Biochemistry and the Department of Radiation Biology and Biophysics, University of Rochester School of Medicine and Dentistry, Rochester, New York 14642, USA
2Department of Radiation Biology and Biophysics University of Rochester School of Medicine and Dentistry Rochester, New York 14642, USA
3Institute for Protein Research, Osaka University, Suita, Osaka 565, Japan

Tóm tắt

AbstractMethionine aminopeptidases with a universal specificity have been revealed from the sequences of the amino‐terminal region of mutant forms of yeast iso‐1‐cytochrome c and from a systematic examination of the literature for amino‐terminal sequences formed at initiation sites. The aminopeptidase removes amino‐terminal residues of methionine when they precede certain amino acids, with a specificity that appears to be determined mainly by the residue adjacent to the methionine residue at the amino terminus. The result with the mutationally altered iso‐1‐cytochromes c and the results from published sequences of other proteins from a wide range of prokaryotes and eukaryotes suggest that the aminopeptidase usually cleaves amino‐terminal methionine when it precedes residues of alanine, cysteine, glycine, proline, serine, threonine and valine but not when it precedes residues of arginine, asparagine, aspartic acid, glutamine, glutamic acid, isoleucine, leucine, lysine or methionine. We suggest that the specificity is almost always determined simply by the size of the side chain of the penultimate residue; methionine is usually cleaved from residues with a side chain having a radius of gyration of 1·29 Å or less, but is not cleaved from residues with larger side chains.

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BioEssays

Tập 3 Số 1

27-31

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