Regulation of protein synthesis factor EF-1 alpha in Mucor racemosus.
Open Access
- 1 May 1985
- journal article
- research article
- Published by Taylor & Francis in Molecular and Cellular Biology
- Vol. 5 (5) , 1100-1103
- https://doi.org/10.1128/mcb.5.5.1100
Abstract
The protein synthesis elongation factor EF-1 alpha of Mucor racemosus hyphae contained eight or nine methylated amino acids per molecule, whereas the factor from sporangiospores was nonmethylated. During the course of spore germination, the specific activity of the factor in crude extracts increased sixfold. This increase in activity was accompanied by a constant level of EF-1 alpha-specific mRNA and a constant level of EF-1 alpha protein. Methylation of the protein, however, accelerated during the germination process, in parallel with the increase in specific activity of the factor. We propose that the activity of EF-1 alpha is regulated during germination through methylation of the protein and does not involve transcriptional regulation.This publication has 27 references indexed in Scilit:
- Methylation of elongation factor 1α in mouse 3T3B and 3T3BSV40 cellsFEBS Letters, 1983
- Sequence homology between EF‐1α, the α‐chain of elongation factor 1 from Artemia salina and elongation factor EF‐TU from Escherichia coliFEBS Letters, 1983
- Cold‐Sensitive Ribosome Assembly in an Esclzerichia coli Mutant Lacking a Single Methyl Group in Ribosomal Protein L3European Journal of Biochemistry, 1981
- Regulation of translation rate during morphogenesis in the fungus MucorBiochemistry, 1978
- High resolution two-dimensional electrophoresis of basic as well as acidic proteinsCell, 1977
- Developmental changes in messenger RNAs and protein synthesis in Dictyostelium discoideumDevelopmental Biology, 1977
- A Rapid and Sensitive Method for the Quantitation of Microgram Quantities of Protein Utilizing the Principle of Protein-Dye BindingAnalytical Biochemistry, 1976
- Methylation of the ribosomal proteins in Escherichia coli. Nature and stoichiometry of the methylated amino acids in 50S ribosomal proteinsBiochemistry, 1975
- 50-S Ribsomal Proteins. Peptide Studies on Two Acidic Proteins, A1 and A2, Isolated from 50-S Ribosomes of Escherichia coliEuropean Journal of Biochemistry, 1972
- Secondary modification of cytochrome c by Neurospora crassaBiochemistry, 1969