Processing of the N termini of nascent polypeptide chains requires deformylation prior to methionine removal
- 1 January 1999
- journal article
- Published by Elsevier BV in Journal of Molecular Biology
- Vol. 290 (3), 607-614
- https://doi.org/10.1006/jmbi.1999.2913
Abstract
No abstract availableKeywords
This publication has 27 references indexed in Scilit:
- Covalent Modification of an Exposed Surface Turn Alters the Global Conformation of the Biotin Carrier Domain of Escherichia coli Acetyl-CoA CarboxylasePublished by Elsevier BV ,1997
- Structure of the biotinyl domain of acetyl-coenzyme A carboxylase determined by MAD phasingStructure, 1995
- A protein catalytic framework with an N-terminal nucleophile is capable of self-activationNature, 1995
- Expression, biotinylation and purification of a biotin-domain peptide from the biotin carboxy carrier protein of Escherichia coli acetyl-CoA carboxylaseBiochemical Journal, 1994
- In vivo processing of N‐terminal methionine in E. coliFEBS Letters, 1990
- Methionine aminopeptidase gene of Escherichia coli is essential for cell growthJournal of Bacteriology, 1989
- Processing of the initiation methionine from proteins: properties of the Escherichia coli methionine aminopeptidase and its gene structureJournal of Bacteriology, 1987
- The fate of norleucine as a replacement for methionine in protein synthesisJournal of Molecular Biology, 1979
- Cleavage of the N-terminal formymlethionine residue from a bacteriophage coat protein in vitroJournal of Molecular Biology, 1973
- On the release of the formyl group from nascent proteinJournal of Molecular Biology, 1968