Gene/Protein Disease Symptom Drug Enzyme Compound
Pivot Concepts:   Target Concepts:
Query: UMLS:C0679427 (myeloblastosis)
 982 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

Cells infected by Rous-associated virus 61 (RAV-61) contained a precursor-like protein, pr90, that was specifically precipitated by antiserum directed against envelope glycoproteins, gp85 and gp35. Tryptic peptide mapping showed that pr90 contained tryptic sequences of both gp85 and gp35. Pactamycin mapping experiments indicated that the two glycoproteins are translated from the env-mRNA in the order (5') gp85--gp35. The pactamycin mapping experiments also indicated a translational order of p10--(p27, p12)--p15 for the gag proteins; this agreement with the order previously reported from tryptic mapping studies on precursor pr76 of avian myeloblastosis virus implied that the stoichiometry of the core proteins was unchanged when virions were assembled in the presence of pactamycin. The reverse transcriptase proteins, unlike those of the env and gag genes, fell on the right side of the pactamycin map. This result is in accord with the idea that most, if not all, of the reverse transcriptase protein is translated by read-through of the gag(pol) message rather than by translation of a hypothetical pol-mRNA devoted solely to synthesis of that protein.
 ...
PMID:Proteins of Rous-associated virus 61, an avian retrovirus: common precursor for glycoproteins gp85 and gp35 and use of pactamycin to map translational order of proteins in the gag, pol, and env genes. 7 10

The isoelectric focusing technique in the pH gradients was used for a preparative isolation of proteins from Rous sarcoma virus and avian myeloblastosis virus. The purified major gs protein, p27 (pI = 9.1) and the gP86 (pI = 5.3) were obtained after disruption of virus with 1% non-ionogenic detergent in the presence of 6M urea. The p10, p15, and p19 were present in the same range of pH (pI = 6.8). A strongly basic protein, immunologically active, presumably the p12, was found in the alkaline region of the pH gradient 10.8. These proteins fully retained their immunological activity. On the other hand, in the acidic region of the pH gradient between pH 4 and 5, strong precipitates were regularly found. These precipitates were complexes which were formed by interaction of the acid components of ampholines with the viral proteins during isoelectric focusing. Almost all viral proteins were present, differing only in quantity. The complexes were stabile in 1% non-inogenic detergent and 6M urea. They were dissociated with 1% SDS and 5M urea, and had no immunological activity. The methods of virus disruption and possibilities of formation of the ampholine-viral protein complexes are discussed.
 ...
PMID:Fractionation of proteins from Rous sarcoma virus and avian myeloblastosis virus by isoelectric focusing. 21 31

The activity of the avian myeloblastosis virus (AMV) or the human immunodeficiency virus type 1 (HIV-1) protease on peptide substrates which represent cleavage sites found in the gag and gag-pol polyproteins of Rous sarcoma virus (RSV) and HIV-1 has been analyzed. Each protease efficiently processed cleavage site substrates found in their cognate polyprotein precursors. Additionally, in some instances heterologous activity was detected. The catalytic efficiency of the RSV protease on cognate substrates varied by as much as 30-fold. The least efficiently processed substrate, p2-p10, represents the cleavage site between the RSV p2 and p10 proteins. This peptide was inhibitory to the AMV as well as the HIV-1 and HIV-2 protease cleavage of other substrate peptides with Ki values in the 5-20 microM range. Molecular modeling of the RSV protease with the p2-p10 peptide docked in the substrate binding pocket and analysis of a series of single-amino acid-substituted p2-p10 peptide analogues suggested that this peptide is inhibitory because of the potential of a serine residue in the P1' position to interact with one of the catalytic aspartic acid residues. To open the binding pocket and allow rotational freedom for the serine in P1', there is a further requirement for either a glycine or a polar residue in P2' and/or a large amino acid residue in P3'. The amino acid residues in P1-P4 provide interactions for tight binding of the peptide in the substrate binding pocket.
 ...
PMID:Mechanism of inhibition of the retroviral protease by a Rous sarcoma virus peptide substrate representing the cleavage site between the gag p2 and p10 proteins. 133 Oct 99

We have purified two low-molecular-weight polypeptides from the Prague C strain of Rous sarcoma virus and have identified these as products of the gag precursor Pr76 by protein sequencing and by amino acid analysis. Both polypeptides are derived from a stretch of 22 amino acids within Pr76 that separates p19 and p10. We refer to this region as p2. Together the two cleavage products form the entire p2 region. The junctions of p19 with the amino-terminal fragment of p2 and of p10 with the carboxy-terminal fragment of p2 define two new processing sites within the gag precursor, Tyr-155-His-156 and Gly-177-Ser-178. Both polypeptides are major cleavage products of Pr76 that occur in Prague C Rous sarcoma virus at an estimated 1,000 copies per virion. They also are prominent components of avian myeloblastosis virus. The combination of gel filtration and reverse-phase high-pressure liquid chromatography, which was used for the isolation of the two fragments of p2, resolved over a dozen other low-molecular-weight polypeptides from avian sarcoma and leukemia viruses that previously were undetected. This technique thus should serve as a useful procedure for further characterization of viral components.
 ...
PMID:Structure and processing of the p2 region of avian sarcoma and leukemia virus gag precursor polyproteins. 300 58

We have developed procedures for the purification of a 6,000-dalton protein from avian myeloblastosis virus. This protein is a major component of avian myeloblastosis virus, accounting for over 7% of total protein, and thus is equimolar with the other internal structural proteins in virions. As described in the accompanying paper (Hunter et al., J. Virol. 45:885-888, 1983), the results of N-terminal amino acid sequence analysis identify the protein as a product of the gag gene. We suggest denoting this protein as p10, according to nomenclature that is already in use for a previously identified but poorly defined low-molecular-weight protein or proteins of avian sarcoma and leukemia viruses. In virions p10 appears to be located between the core and the membrane. Several of its properties may explain why p10 has not been characterized previously. Among these are its abnormal amino acid composition, its solubility under conditions where most proteins are fixed into sodium dodecyl sulfate-polyacrylamide gels, and the variability in its electrophoretic migration in different avian sarcoma viruses.
 ...
PMID:Purification and properties of a fifth major viral gag protein from avian sarcoma and leukemia viruses. 630 Apr 27

We have identified p10 as a fifth gag protein of avian sarcoma and leukemia viruses. Amino-terminal protein sequencing of this polypeptide purified from the Prague C strain of Rous sarcoma virus and from avian myeloblastosis virus implies that it is encoded within a stretch of 64 amino acid residues between p19 and p27 on the gag precursor polypeptide. For p10 from the Prague C strain of Rous sarcoma virus the first 30 residues were found to be identical with the predicted amino acid sequence from the Prague C strain of Rous sarcoma virus DNA sequence, whereas for p10 from avian myeloblastosis virus the protein sequence for the same region showed two amino acid substitutions. Amino acid composition data indicate that there are no gross composition changes beyond the region sequenced. The amino terminus of p10 is located two amino acid residues past the carboxy terminus of p19, whereas its carboxy terminus probably is located immediately adjacent to the first amino acid residue of p27.
 ...
PMID:Amino-terminal amino acid sequence of p10, the fifth major gag polypeptide of avian sarcoma and leukemia viruses. 630 Apr 42