Molecular basis of the altered gag p19 protein (MA) of the transformation-defective mutant of Rous sarcoma virus, tdPH2010. 1997

H Hara, and T Tanabe, and A Kaji
Department of Microbiology, University of Pennsylvania School of Medicine, Philadelphia 19104, USA.

The transformation-defective mutant of Rous sarcoma virus (RSV), tdPH2010, has a gag p19 (matrix; MA) protein which migrates on SDS-polyacrylamide gels faster than that of the parental (tsNY68) as well as other wild-type strains of RSV. To study the molecular basis of this altered migration pattern and its biological significance, the nucleotide sequence of the p19 region of tdPH2010 was determined. Comparison of the nucleotide sequence of tdPH2010 with that of the Schmidt-Ruppin A strain of RSV revealed a point mutation at nucleotide 755 (G to A), resulting in an amino-acid substitution at residue 126 of p19 (Glu to Lys). Acidic-methanol esterification of free carboxyl groups suppressed the difference in electrophoretic mobility of p19 between tdPH2010 and the wild-type virus. Recombinant virus constructs having the mutated gag region of tdPH2010 produced a p19 with the same electrophoretic mobility as the p19 of tdPH2010. We concluded that the point mutation caused the altered electrophoretic behavior of p19 of tdPH2010. The mutation had no effect on the growth of infected cells.

UI MeSH Term Description Entries
D008969 Molecular Sequence Data Descriptions of specific amino acid, carbohydrate, or nucleotide sequences which have appeared in the published literature and/or are deposited in and maintained by databanks such as GENBANK, European Molecular Biology Laboratory (EMBL), National Biomedical Research Foundation (NBRF), or other sequence repositories. Sequence Data, Molecular,Molecular Sequencing Data,Data, Molecular Sequence,Data, Molecular Sequencing,Sequencing Data, Molecular
D011994 Recombinant Proteins Proteins prepared by recombinant DNA technology. Biosynthetic Protein,Biosynthetic Proteins,DNA Recombinant Proteins,Recombinant Protein,Proteins, Biosynthetic,Proteins, Recombinant DNA,DNA Proteins, Recombinant,Protein, Biosynthetic,Protein, Recombinant,Proteins, DNA Recombinant,Proteins, Recombinant,Recombinant DNA Proteins,Recombinant Proteins, DNA
D003588 Cytopathogenic Effect, Viral Visible morphologic changes in cells infected with viruses. It includes shutdown of cellular RNA and protein synthesis, cell fusion, release of lysosomal enzymes, changes in cell membrane permeability, diffuse changes in intracellular structures, presence of viral inclusion bodies, and chromosomal aberrations. It excludes malignant transformation, which is CELL TRANSFORMATION, VIRAL. Viral cytopathogenic effects provide a valuable method for identifying and classifying the infecting viruses. Cytopathic Effect, Viral,Viral Cytopathogenic Effect,Cytopathic Effects, Viral,Cytopathogenic Effects, Viral,Effect, Viral Cytopathic,Effect, Viral Cytopathogenic,Effects, Viral Cytopathic,Effects, Viral Cytopathogenic,Viral Cytopathic Effect,Viral Cytopathic Effects,Viral Cytopathogenic Effects
D004591 Electrophoresis, Polyacrylamide Gel Electrophoresis in which a polyacrylamide gel is used as the diffusion medium. Polyacrylamide Gel Electrophoresis,SDS-PAGE,Sodium Dodecyl Sulfate-PAGE,Gel Electrophoresis, Polyacrylamide,SDS PAGE,Sodium Dodecyl Sulfate PAGE,Sodium Dodecyl Sulfate-PAGEs
D004951 Esterification The process of converting an acid into an alkyl or aryl derivative. Most frequently the process consists of the reaction of an acid with an alcohol in the presence of a trace of mineral acid as catalyst or the reaction of an acyl chloride with an alcohol. Esterification can also be accomplished by enzymatic processes. Esterifications
D000595 Amino Acid Sequence The order of amino acids as they occur in a polypeptide chain. This is referred to as the primary structure of proteins. It is of fundamental importance in determining PROTEIN CONFORMATION. Protein Structure, Primary,Amino Acid Sequences,Sequence, Amino Acid,Sequences, Amino Acid,Primary Protein Structure,Primary Protein Structures,Protein Structures, Primary,Structure, Primary Protein,Structures, Primary Protein
D001358 Avian Sarcoma Viruses Group of alpharetroviruses (ALPHARETROVIRUS) producing sarcomata and other tumors in chickens and other fowl and also in pigeons, ducks, and RATS. Avian Sarcoma Virus B77,Chicken Sarcoma Virus B77,Chicken Tumor 1 Virus,Fujinami sarcoma virus,Sarcoma Viruses, Avian,Avian Sarcoma Virus,Fujinami sarcoma viruses,Sarcoma Virus, Avian,Virus, Avian Sarcoma,Viruses, Avian Sarcoma,sarcoma virus, Fujinami,virus, Fujinami sarcoma,viruses, Fujinami sarcoma
D001483 Base Sequence The sequence of PURINES and PYRIMIDINES in nucleic acids and polynucleotides. It is also called nucleotide sequence. DNA Sequence,Nucleotide Sequence,RNA Sequence,DNA Sequences,Base Sequences,Nucleotide Sequences,RNA Sequences,Sequence, Base,Sequence, DNA,Sequence, Nucleotide,Sequence, RNA,Sequences, Base,Sequences, DNA,Sequences, Nucleotide,Sequences, RNA
D015683 Gene Products, gag Proteins coded by the retroviral gag gene. The products are usually synthesized as protein precursors or POLYPROTEINS, which are then cleaved by viral proteases to yield the final products. Many of the final products are associated with the nucleoprotein core of the virion. gag is short for group-specific antigen. Viral gag Proteins,gag Antigen,gag Gene Product,gag Gene Products,gag Polyproteins,gag Protein,gag Viral Proteins,Gene Product, gag,Retroviral Antigen gag Protein,gag Antigens,gag Gene Related Protein,gag Polyprotein,Antigen, gag,Antigens, gag,Polyprotein, gag,Polyproteins, gag,Protein, gag,Proteins, Viral gag,Proteins, gag Viral,Viral Proteins, gag,gag Proteins, Viral
D017353 Gene Deletion A genetic rearrangement through loss of segments of DNA or RNA, bringing sequences which are normally separated into close proximity. This deletion may be detected using cytogenetic techniques and can also be inferred from the phenotype, indicating a deletion at one specific locus. Deletion, Gene,Deletions, Gene,Gene Deletions

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