Gene/Protein Disease Symptom Drug Enzyme Compound
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Query: UNIPROT:Q07644 (polypeptide)
 72,197 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

It was previously shown that virus-specific polypeptides made in HEp-2 cells infected with herpes simplex 1 form three groups designated alpha, beta, and gamma whose synthesis is coordinately regulated and sequentially ordered. This report shows that one or more functional alpha polypeptides are necessary to turn on the synthesis of beta and gamma groups, and conversely, one or more polypeptides in the latter groups turn off the synthesis of alpha polypeptides. Specifically, infected cells maintained in medium containing either canavanine, an analogue of arginine, or azetidine-2-carboxylic acid an analogue of proline and hydroxyproline, synthesized alpha polypeptide at rates comparable to maximal rates in untreated infected cells but did not undergo the normal transition to beta and gamma polypeptide synthesis. The transition to gamma polypeptide synthesis and shut-off of synthesis of earlier polypeptide groups proceeded normally if addition of canavanine was delayed until at least 4-5 hr after infection. Addition of canavanine after the onset of beta and gamma polypeptide synthesis, i.e., between 2 and 3.5 hr after infection, resulted in sustained, simultaneous synthesis of all three polypeptide groups, a phenomenon not seen in untreated infected cells. Canavanine-treated infected cells, synthesizing alpha polypeptides, recovered the capacity to make beta and gamma polypeptides after removal of the analogue, but only after a 1-to 2-hr delay compared with infected untreated cells. The data indicate that the on and off controls inherent in the cascade regulation of viral polypeptide synthesis are mediated by one or more polypeptides in each group at transcriptional or post-transcriptional levels.
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PMID:Regulation of herpesvirus macromolecular synthesis: sequential transition of polypeptide synthesis requires functional viral polypeptides. 16 3

Many of the 200 or so non-protein amino acids synthesized by higher plants are related structurally to the constituents of common proteins. L-Canavanine, the guanidinooxy structural analogue of L-arginine, is representative of this group. It has provided valuable insight into the biological effects and the mode of action of non-protein amino acids which acts as analogues of the protein amino acids. The arginyl-tRNA synthetases of numerous canavanine-free species charge canavanine, and canavanine is subsequently incorporated into the nascent polypeptide chain. Production of canavanine-containing proteins ultimately can disrupt critical reactions of RNA and DNA metabolism as well as protein synthesis. Canavanine also affects regulatory and catalytic reactions of arginine metabolism, arginine uptake, formation of structural components, and other cellular precesses. In these ways, canavanine alters essential biochemical reactions and becomes a potent antimetabolite of arginine in a wide spectrum of species. These deleterious properties of canavanine render it a highly toxic secondary plant constituent that probably functions as an allelochemic agent that deters the feeding activity of phytophagous insects and other herbivores.
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PMID:The biological effects and mode of action of L-canavanine, a structural analogue of L-arginine. 33 85

L-Canavanine is a potentially deleterious arginine antimetabolite whose toxicity is expressed in canavanine-sensitive organisms ranging from viruses to humans. Canavanine, a substrate for arginyl-tRNA synthetase, is incorporated into nascent polypeptide chains in place of arginine. This substitution results in the production of structurally aberrant, canavanyl proteins. Chemical, physical, and immunological studies of native and canavanine-containing vitellogenin obtained from female migratory locusts (Locusta migratoria migratorioides (Orthoptera] provide the first experimental evidence that canavanine can disrupt the tertiary and/or quaternary structure that yields the three-dimensional conformation unique to the protein. These findings enhance our understanding of the biochemical basis for canavanine's antimetabolic and potent insecticidal properties.
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PMID:L-canavanine incorporation into vitellogenin and macromolecular conformation. 276 38

L-Canavanine, a nonprotein amino acid of certain leguminous plants, manifests potent insecticidal properties in a canavanine-sensitive insect such as the tobacco hornworm Manduca sexta (L.) (Sphingidae). This arginine analog is activated and aminoacylated by arginyl-tRNA synthetase and incorporated into nascent polypeptide chains to create structurally aberrant, canavanine-containing proteins. Analysis of incorporation of [3H]leucine into protein in M. sexta larvae that had been injected with canavanine revealed that this arginine analog stimulates protein synthesis. During the first 3 hr after injection of canavanine, canavanine-mediated net stimulation of protein formation was readily discerned. Thereafter, the stimulation of protein synthesis appeared to be offset by the preferential degradation of anomalous proteins. Double-label protein-turnover experiments with larvae injected with [14C]canavanine- and [3H]arginine-containing hemolymph proteins showed that canavanine-containing proteins were degraded preferentially.
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PMID:L-Canavanine and protein synthesis in the tobacco hornworm Manduca sexta. 345 53

Cultured rat embryo cells exposed to the L-arginine analogue L-canavanine rapidly accumulated a major 71 kilodalton polypeptide and several minor ones (110, 95, 88, and 78 kilodaltons). Canavanine-treated cultures contained elevated levels of translatable mRNA encoding P71, and the stimulated synthesis of this protein was blocked by actinomycin D, suggesting that P71 is inducible. Rat embryo cells maintained under routine culture conditions synthesized only trace amounts of P71; however, they accumulated an abundant 73 kilodalton protein that was closely related to P71. No kinetic evidence of a precursor-product relationship between P73 and P71 was found. The peptide map of P71 from cultured cells was identical to the map of proteins with the same electrophoretic mobility isolated from incubated slices of rat telencephalon. Previous studies (White, '80a, b, c) have shown that the latter proteins are rapidly synthesized by cells associated with cerebral microvessels in incubated brain slices, but are not detectable in vivo. Herein we present evidence that the synthesis of P71 is not unique to brain slices. Incubated slices of heart, lung, thymus, kidney, spleen, and liver all accumulated an abundant 71 kilodalton size class. The peptide maps of P71 obtained from brain, heart, lung and thymus tissue were similar. The stimulated synthesis of P71 in brain, heart, and lung slices was inhibited strongly by the addition of actinomycin D at the start of incubation. The 71-73 kilodalton proteins of canavanine-treated rat embryo cells and incubated slices from seven different organs were compared in detail on two-dimensional polyacrylamide gels. Eight charge variants were detected in extracts of lung, spleen, and thymus tissue, four in liver and heart, three in kidney, and two different pairs of variants in extracts of brain tissue and cultured cells. The possible significance of the rapid synthesis of a similar small set of proteins in tissue slices and cultured cells in response to a variety of physical, chemical, and biological stimuli is discussed in terms of cellular responses to traumatic injury and metabolic stress.
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PMID:Cellular responses to stress: comparison of a family of 71--73-kilodalton proteins rapidly synthesized in rat tissue slices and canavanine-treated cells in culture. 726 72

Canavanine is an arginine analog which is widely used to inhibit proteolytic processing of viral polyproteins. Certain results obtained with canavanine have suggested that it may have other effects. Therefore, we examined the effects of canavanine on the cell-free synthesis of murine retrovirus proteins. It was found that the electrophoretic mobility of the major gag-related cell-free product of both Rauscher murine leukemia virus (R-MuLV) and Moloney murine sarcoma virus 124 (Mo-MuSV-124) RNA was dependent on the concentration of canavanine used during translation. As the canavanine concentration was increased up to 4 mM, the apparent size of the major gag-related polypeptide also increased from 65,000 (R-MuLV RNA) or 63,000 (Mo-MuSV-124 RNA) to approximately 80,000 daltons. Additional increases in the canavanine concentration up to 12 mM did not increase the size of the gag gene product beyond 80,000 daltons. This change in electrophoretic mobility appeared to be due to a substitution of canavanine for arginine residues in the polypeptides, not to a change in their actual size. If amber suppressor tRNA and canavanine were used together during translation of Mo-MuSV-124 RNA and Mo-MuLV RNA, the results were also in agreement with this proposal. Translation experiments done with ovalbumin mRNA and mengovirus 35S RNA indicated that canavanine incorporation caused a shift in the electrophoretic mobility of ovalbumin from 43,000 to 45,000 daltons and caused the appearance of two slightly larger polypeptides in the 155,000- and 115,000- dalton regions of the mengovirus RNA cell-free product.
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PMID:Effect of canavanine on murine retrovirus polypeptide formation. 736 78

L-Canavanine manifests potent insecticidal properties in a canavanine-sensitive insect such as the tobacco hornworm,Manduca sexta (L.) (Sphingidae). Investigations of the biochemical basis for the antimetabolic properties of this arginine analog reveal that it is activated and aminoacylated by arginyl tRNA synthetase and incorporated into the nascent polypeptide chain. This creates structurally aberrant, canavanine-containing proteins that can possess altered physicochemical properties. Evidence is presented in studies with the tobacco hornworm; the canavanine-adapted bruchid beetle,Caryedes brasiliensis (Bruchidae) and the weevil,Sternechus tuberculatus (Curculionidae); as well as the canavanine-resistant larvae ofHeliothis virescens [Noctuidae] to support the contention that formation of aberrant, canavanyl proteins produce deleterious biological effects and is a significant basis for canavanine's antimetabolic properties.
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PMID:Biochemical insight into insecticidal properties ofL-Canavanine, a higher plant protective allelochemical. 2430 52