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Nonuniform Size Distribution Of Nascent Globin Peptides, Evidence For Pause Localization Sites, And A Cotranslational Protein-folding Model
I. Krasheninnikov, A. A. Komar, I. Adzhubei
Published 1991 · Chemistry, Medicine
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Examination of nascent globin peptides accumulatingin vitro during globin synthesis in rabbit reticulocyte lysates was carried out. A view was supported that nonrandom distribution of codons with different usage frequencies in mRNA may determine the messenger's translation kinetics. Regions of reduced translation of α- and β-globin polypeptide chains were localized, and the cotranslational protein-folding model suggested previously was substantiated. An active conjunction of synthesis and folding of proteins was proposed as one of the main destinations of a translation nonuniformity.
This paper references
Sense codons are found in specific contexts.
M. Yarus (1985)
Variable rate of polypeptide chain elongation for colicins A, E2 and E3.
S. Varenne (1982)
Role of primary structure and disulfide bond formation in beta-lactamase secretion.
S. Pollitt (1983)
The primary structure of the Saccharomyces cerevisiae gene for alcohol dehydrogenase.
J. Bennetzen (1982)
Novel intermediates in the synthesis of maltose-binding protein in Escherichia coli.
L. Randall (1980)
Variable rate of polypeptide chain elongation in vitro. Effect of spermidine.
A. K. Abraham (1980)
Codon usage in yeast: cluster analysis clearly differentiates highly and lowly expressed genes
P. Sharp (1986)
Tricine-sodium dodecyl sulfate-polyacrylamide gel electrophoresis for the separation of proteins in the range from 1 to 100 kDa.
H. Schägger (1987)
Isolation and amino acid sequence of a monomeric hemoglobin in heart muscle of the bullfrog, Rana catesbeiana.
N. Maeda (1982)
Gel chromatographic analysis of nascent globin chains. Evidence of nonuniform size distribution.
A. Protzel (1974)
Correlation between the abundance of yeast transfer RNAs and the occurrence of the respective codons in protein genes. Differences in synonymous codon choice patterns of yeast and Escherichia coli with reference to the abundance of isoaccepting transfer RNAs.
T. Ikemura (1982)
Does the channel for nascent peptide exist inside the ribosome? Immune electron microscopy study
L. Ryabova (1988)
Reticulocyte transfer RNA and hemoglobin synthesis
D. W. Smith (1975)
DNA sequences from the str operon of Escherichia coli.
L. Post (1980)
Translational pauses during a spider fibroin synthesis.
G. Candelas (1983)
INDUCED ENZYME FORMED ON BACTERIAL POLYRIBOSOMES.
Y. Kiho (1964)
Nonrandom utilization of codon pairs in Escherichia coli.
G. Gutman (1989)
Polypeptide chain folding through a highly helical intermediate as a general principle of globular protein structure formation
V. Lim (1978)
Globin synthesis on reticulocyte membrane-bound ribosomes.
W. Woodward (1973)
[Is there a channel for a peptide synthesized on a ribosome? Labeling of translating ribosomes with atomic tritium].
V. Kolb (1987)
Complementation on Ribosomes
D. Zipser (1963)
An efficient mRNA-dependent translation system from reticulocyte lysates.
H. Pelham (1976)
Formation of an intrachain disulfide bond on nascent immunoglobulin light chains.
L. W. Bergman (1979)
The efficiency of folding of some proteins is increased by controlled rates of translation in vivo. A hypothesis.
I. J. Purvis (1987)
Correlation between the abundance of Escherichia coli transfer RNAs and the occurrence of the respective codons in its protein genes: a proposal for a synonymous codon choice that is optimal for the E. coli translational system.
T. Ikemura (1981)
Co-translational modification of nascent immunoglobulin heavy and light chains.
L. W. Bergman (1979)
Competition between alpha- and beta-globin messenger ribonucleic acids for eucaryotic initiation factor 2.
G. Di Segni (1979)
Nonuniform size distribution of nascent peptides. The effect of messenger RNA structure upon the rate of translation.
William G. Chaney (1979)
[Role of the rare codon clusters in defining the boundaries of polypeptide chain regions with identical secondary structures in the process of co-translational folding of proteins].
I. Krasheninnikov (1988)
[Frequency of using codons in mRNA and coding of the domain structure of proteins].
I. Krasheninnikov (1989)
The secondary structure of mRNAs from Escherichia coli: its possible role in increasing the accuracy of translation
E. G. Shpaer (1985)
Codon selection in yeast.
J. Bennetzen (1982)
Regulation of hemoglobin synthesis. Equal rates of translation and termination of - and -globin chains.
H. Lodish (1972)
Ribosome pausing and stacking during translation of a eukaryotic mRNA.
S. Wolin (1988)
Specialization of Rabbit Reticulocyte Transfer RNA Content for Hemoglobin Synthesis
D. W. Smith (1971)
Formation of intermolecular disulfide bonds on nascent immunoglobulin polypeptides.
L. W. Bergman (1979)
Biosynthesis and Assembly of Immunoglobulin G
B. Askonas (1967)
Discontinuous translation of silk fibroin in a reticulocyte cell-free system and in intact silk gland cells.
P. Lizardi (1979)
Constraints on codon context in Escherichia coli genes. Their possible role in modulating the efficiency of translation.
E. G. Shpaer (1986)
Atlas of protein sequence and structure
M. A. Chang (1965)
Preferential codon usage in prokaryotic genes: the optimal codon-anticodon interaction energy and the selective codon usage in efficiently expressed genes.
H. Grosjean (1982)
The biosynthesis of rat serum albumin. In vivo studies on the formation of the disulfide bonds.
Theodore Peters (1982)
Features of the cell-free translation of a spider fibroin mRNA.
G. Candelas (1989)
Codon choice and gene expression: synonymous codons differ in their ability to direct aminoacylated-transfer RNA binding to ribosomes in vitro.
L. K. Thomas (1988)
This paper is referenced by
A pause for thought along the co-translational folding pathway.
A. Komar (2009)
Assembly of Tropomyosin Isoforms into the Cytoskeleton of Avian Muscle Cells
T. L'ecuyer (1998)
Codon bias and heterologous protein expression.
Claes Gustafsson (2004)
In silico methods for co-transcriptional RNA secondary structure prediction and for investigating alternative RNA structure expression.
I. Meyer (2017)
Conformational diseases: Looking into the eyes
A. Surguchev (2010)
Synonymous codon usage influences the local protein structure observed
R. Saunders (2010)
Mapping codon usage of the translation initiation region in porcine reproductive and respiratory syndrome virus genome
Jun-hong Su (2011)
Birth, life and death of nascent polypeptide chains
Sujata S Jha (2011)
Analysis of distribution indicates diverse functions of simple sequence repeats in Mycoplasma genomes.
J. Mrázek (2006)
Cotranslational folding of proteins.
Basharov Ma (2000)
Cotranslational heme binding to nascent globin chains
A. Komar (1993)
Clustering of Codons with Rare Cognate tRNAs in Human Genes Suggests an Extra Level of Expression Regulation
Joanna L. Parmley (2009)
Investigations into the relationship between evolutionary rate variation, protein structure and codon usage
Louis du Plessis (2011)
Evidence of rare codon clusters within Escherichia coli coding regions.
D. Phoenix (1997)
Non‐random usage of ‘degenerate’ codons is related to protein three‐dimensional structure
Alexei A. Adzhubei (1996)
Specific correlations between relative synonymous codon usage and protein secondary structure.
M. Orešič (1998)
Co-translational mechanisms of quality control of newly synthesized polypeptides
V. Gandin (2014)
Elongation Rate and its Modulation
A. Spirin (1999)
Protein structure and the sequential structure of mRNA: α‐Helix and β‐sheet signals at the nucleotide level
S. Brunak (1996)
The effect of a hydrophobic N-terminal probe on translational pausing of chloramphenicol acetyl transferase and rhodanese.
T. Tsalkova (1999)
Large-scale analysis of conserved rare codon clusters suggests an involvement in co-translational molecular recognition events
M. Chartier (2012)
A historical perspective on gene/protein functional assignment
C. Hodgman (2000)
Distribution of Rare Triplets Along mRNA and Their Relation to Protein Folding
Cameel H Makhoul (2002)
Silent SNPs: impact on gene function and phenotype.
A. Komar (2007)
Kinetics of translation of γB crystallin and its circularly permutated variant in an in vitro cell‐free system: possible relations to codon distribution and protein folding
A. Komar (1995)
Segmented Genome: Elementary Units of Genome Structure
E. Trifonov (2004)
Protein secondary structural types are differentially coded on messenger RNA
T. Thanaraj (1996)
Investigating the role of site specific synonymous variation in disease association studies.
A. Bhardwaj (2014)
The signal recognition particle receptor alpha subunit assembles co‐translationally on the endoplasmic reticulum membrane during an mRNA‐encoded translation pause in vitro.
J. Young (1996)
Synonymous Codon Usage—a Guide for Co-Translational Protein Folding in the Cell
A. A. Komar (2019)
Cotranslational Folding of Globin*
A. Komar (1997)
The imprint of codons on protein structure
C. Deane (2011)See more