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Genes encoding the core proteins of adenovirus type 2. 1984

P Aleström, and G Akusjärvi, and M Lager, and L Yeh-kai, and U Pettersson

The nucleotide sequence of the HindIII-D fragment of adenovirus type 2 has been determined. The sequence, which is located between coordinates 41.8 and 51.0, covers most of the L2 cotermination family. It includes three major open translational reading frames encoding the carboxyl-terminal part of the penton base as well as the major core polypeptides V and VII. An additional minor open translational reading frame encoding a highly basic polypeptide was detected in the sequence. The L2 region has a very compact organization with very short distances between the different genes, although no overlapping coding sequences were found. The predicted amino acid sequences of core proteins V and VII reveal that they are highly basic proteins and polypeptide VII resembles the arginine-rich H4 histones in its amino acid composition, but no striking similarities are apparent at the amino acid sequence level. The candidate polypeptide encoded by the newly discovered translational reading frame contains 29% basic residues and includes a hypothetical recognition sequence for the adenovirus-encoded endopeptidase. In conjunction with previously published sequences and those reported in accompanying papers (Akusjärvi, G., Aleström, P., Pettersson, M., Lager, M., Jörnvall, H., and Pettersson, U. (1984) J. Biol. Chem. 259, 13976-13979; Roberts, R. J., O'Neill, K. E., and Yen, C. E. (1984) J. Biol. Chem. 259, 13965-13975) a complete sequence can now be reconstructed for the 35,937-base pairs adenovirus type 2 genome.

UI MeSH Term Description Entries
D009690 Nucleic Acid Conformation The spatial arrangement of the atoms of a nucleic acid or polynucleotide that results in its characteristic 3-dimensional shape. DNA Conformation,RNA Conformation,Conformation, DNA,Conformation, Nucleic Acid,Conformation, RNA,Conformations, DNA,Conformations, Nucleic Acid,Conformations, RNA,DNA Conformations,Nucleic Acid Conformations,RNA Conformations
D004262 DNA Restriction Enzymes Enzymes that are part of the restriction-modification systems. They catalyze the endonucleolytic cleavage of DNA sequences which lack the species-specific methylation pattern in the host cell's DNA. Cleavage yields random or specific double-stranded fragments with terminal 5'-phosphates. The function of restriction enzymes is to destroy any foreign DNA that invades the host cell. Most have been studied in bacterial systems, but a few have been found in eukaryotic organisms. They are also used as tools for the systematic dissection and mapping of chromosomes, in the determination of base sequences of DNAs, and have made it possible to splice and recombine genes from one organism into the genome of another. EC 3.21.1. Restriction Endonucleases,DNA Restriction Enzyme,Restriction Endonuclease,Endonuclease, Restriction,Endonucleases, Restriction,Enzymes, DNA Restriction,Restriction Enzyme, DNA,Restriction Enzymes, DNA
D004279 DNA, Viral Deoxyribonucleic acid that makes up the genetic material of viruses. Viral DNA
D004720 Endonucleases Enzymes that catalyze the hydrolysis of the internal bonds and thereby the formation of polynucleotides or oligonucleotides from ribo- or deoxyribonucleotide chains. EC 3.1.-. Endonuclease
D000260 Adenoviruses, Human Species of the genus MASTADENOVIRUS, causing a wide range of diseases in humans. Infections are mostly asymptomatic, but can be associated with diseases of the respiratory, ocular, and gastrointestinal systems. Serotypes (named with Arabic numbers) have been grouped into species designated Human adenovirus A-G. APC Viruses,APC Virus,Adenovirus, Human,Human Adenovirus,Human Adenoviruses
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
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
D014758 Viral Core Proteins Proteins found mainly in icosahedral DNA and RNA viruses. They consist of proteins directly associated with the nucleic acid inside the NUCLEOCAPSID. Core Proteins, Viral,Major Core Protein,Major Core Proteins, Viral,Adenovirus Core Protein VII,Core Protein V,Core Protein lambda 2,Influenza Virus Core Proteins,Major Core Protein lambda 1,Major Core Protein lambda-1,Major Core Protein sigma 2,Major Core Protein sigma-2,OVP 19,Oncornaviral Protein P19,P30 Core Proteins,Viral Protein P19,Virus Core Proteins,Core Protein, Major,Core Proteins, P30,Core Proteins, Virus,Protein P19, Oncornaviral,Protein P19, Viral,Protein, Major Core,Proteins, P30 Core,Proteins, Viral Core,Proteins, Virus Core
D014764 Viral Proteins Proteins found in any species of virus. Gene Products, Viral,Viral Gene Products,Viral Gene Proteins,Viral Protein,Protein, Viral,Proteins, Viral
D015247 Deoxyribonuclease HindIII One of the Type II site-specific deoxyribonucleases (EC 3.1.21.4). It recognizes and cleaves the sequence A/AGCTT at the slash. HindIII is from Haemophilus influenzae R(d). Numerous isoschizomers have been identified. EC 3.1.21.-. DNA Restriction Enzyme HindIII,Deoxyribonuclease BstFI,Deoxyribonuclease EcoVIII,Endonuclease HindIII,B Pertussis Restriction Enzyme I,BpeI Endonuclease,Endodeoxyribonuclease BpeI,Endonuclease Asp52I,Endonuclease BbrI,Endonuclease BpeI,Endonuclease BstFI,Endonuclease Cfr32I,Endonuclease ChuI,Endonuclease Eco65I,Endonuclease Eco98I,Endonuclease EcoVIII,Endonuclease Hin1076III,Endonuclease Hin173I,Endonuclease HinJCII,Endonuclease HinbIII,Endonuclease HinfII,Endonuclease HsuI,Endonuclease LlaCI,Endonuclease MkiI,LlaCI, Endonuclease

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