Evolution and the distribution of glutaminyl and asparaginyl residues in proteins.
نویسنده
چکیده
Recent experiments on the deamidation of glutaminyl and asparaginyl residues in peptides and proteins support the hypothesis that these residues may serve as molecular clocks that control biological processes. A hypothesis is now offered that suggests that these molecular clocks are set by rejection or accumulation of appropriate sequences of residues including a glutaminyl or asparaginyl residue during evolution.
منابع مشابه
Deamidation of human proteins.
Deamidation of asparaginyl and glutaminyl residues causes time-dependent changes in charge and conformation of peptides and proteins. Quantitative and experimentally verified predictive calculations of the deamidation rates of 1,371 asparaginyl residues in a representative collection of 126 human proteins have been performed. These rates suggest that deamidation is a biologically relevant pheno...
متن کاملNonenzymatic deamidation of asparaginyl and glutaminyl residues in proteins.
Some asparagine and glutamine residues in proteins undergo deamidation to aspartate and glutamate with rates that depend upon the sequence and higher-order structure of the protein. Functional groups within the protein can catalyze this reaction, acting as general acids, bases, or stabilizers of the transition state. Information from specific proteins that deamidate and analysis of protein sequ...
متن کاملMolecular clocks.
A convenient and precise mass spectrometric method for measurement of the deamidation rates of glutaminyl and asparaginyl residues in peptides and proteins has been developed; the rates of deamidation of 306 asparaginyl sequences in model peptides at pH 7.4, 37.0 degrees C, 0.15 M Tris.HCl buffer have been determined; a library of 913 amide-containing peptides for use by other investigators in ...
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The liberation of ammonia in the reaction of transferrin and ascorbic acid in phosphate buffer at pH 7.4, 37°C was investigated. It was found that transferrin is degraded in the reaction into smaller molecular weight polypeptides. The ammonia evolution was inhibited by catalase and by hydroxyl free radical trapping agents such as benzene, benzoate, and iodide. Dehydroascorbic acid and hydrogen ...
متن کاملHuman asparaginyl-tRNA synthetase: molecular cloning and the inference of the evolutionary history of Asx-tRNA synthetase family.
We have cloned and sequenced a cDNA encoding human cytoplasmic asparaginyl-tRNA synthetase (AsnRS). The N-terminal appended domain of 112 amino acid represents the signature sequence for the eukaryotic AsnRS and is absent from archaebacterial or eubacterial enzymes. The canonical ortholog for AsnRS is absent from most archaebacterial and some eubacterial genomes, indicating that in those organi...
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عنوان ژورنال:
- Proceedings of the National Academy of Sciences of the United States of America
دوره 71 3 شماره
صفحات -
تاریخ انتشار 1974