Journal ArticleDOI
Kinetics of maturation of the amino termini of the cell proteins of Escherichia coli
TLDR
The translation time of an average cell protein appears relatively uninfluenced by the presence or absence of growth per se, and many N-termini of cell proteins are stably formylated, and can be isolated intact from cell protein more than a generation after synthesis.About:
This article is published in Biochimica et Biophysica Acta.The article was published on 1969-01-21. It has received 45 citations till now. The article focuses on the topics: Methionine & Ribosomal protein.read more
Citations
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Journal ArticleDOI
Processing of the initiation methionine from proteins: properties of the Escherichia coli methionine aminopeptidase and its gene structure.
TL;DR: In vitro analyses with purified enzyme indicated that MAP is a metallo-oligopeptidase with absolute specificity for the amino-terminal methionine, consistent with the deduced specificity of the enzyme based on the analysis of known amino- terminal sequences of intracellular proteins.
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The ribosome as a platform for co-translational processing, folding and targeting of newly synthesized proteins
TL;DR: The early co-translational events involving the ribosome that guide cytosolic proteins to their native state are reviewed.
Journal ArticleDOI
Protein N-terminal methionine excision.
TL;DR: N-Terminal methionine excision is the major proteolytic pathway responsible for the diversity of N-terminal amino acids in proteins and plays an important role in controlling protein turnover.
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Methionine as translation start signal: A review of the enzymes of the pathway in Escherichia coli
TL;DR: This review focuses on the present knowledge of the five enzymes sustaining the methionine pathway in translation initiation in Escherichia coli: methionyl-tRNA synthetase, methiony-t RNA(fMet) formyltransferase, peptidyl- tRNA hydrolase, Peptide deformylase and methionin aminopeptidase.
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Analysis of the distribution of charged residues in the N-terminal region of signal sequences: implications for protein export in prokaryotic and eukaryotic cells.
TL;DR: A statistical analysis of the distribution of charged residues in the N‐terminal region of 39 prokaryotic and 134 eukaryotic signal sequences reveals a remarkable similarity between the two samples, and suggests that the formyl group on Metf is not removed in prokarian signal sequences.
References
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Book
Methods of Biochemical Analysis
TL;DR: The Radiation Inactivation Method as a Tool to Study Structure-Function Relationships in Proteins Immunoassay with Electrochemical Detection and Theory and Newer Technology Assays for Superoxide Dismutase are studied.
Journal ArticleDOI
Evidence for nonidentical chains in the beta-galactosidase of escherichia coli k12.
Journal ArticleDOI
The purification of aspartate transcarbamylase of Escherichia coli and separation of its protein subunits.
John C. Gerhart,Hella Holoubek +1 more
TL;DR: Purified aspartate transcarbamylase was dissociated by treatment with p-hydroxymercuribenzoate to yield two kinds of protein subunits which were separated by column chromatography and retained their functional properties.
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The role of N-formyl-methionyl-sRNA in protein biosynthesis
B. F. C. Clark,K. A. Marcker +1 more
TL;DR: Bacterial sRNA has been fractionated into two methionine-accepting species, only one of which could be formylated, and the analysis of this polypeptide product identified methionines in internal positions.
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N-Formyl-methionyl-S-RNA
K. A. Marcker,Frederick Sanger +1 more
TL;DR: It has been demonstrated that, after the initial attachment to its specific S-RNA, the free α-amino group of the attached methionine may become formylated.