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D M Rekosh

Publications and source records attributed to D M Rekosh.

27 records · Page 2Linked to original sources
PubMed1982

Expression of the gene encoding the adenovirus DNA terminal protein precursor in productively infected and transformed cells.

The major product of in vitro translation of early RNA prepared from H5ts125-infected cells and selected by hybridization to adenoviral DNA fragments spanning the region from 14.7 to 31.5 map units had been shown to be identical to the 87-kilodalton terminal protein precursor. A 72- to 75-kilodalton polypeptide whose rRNA can be selected by DNA from this same region and made in the presence of anisomycin was indistinguishable from the 72-kilodalton single-stranded DNA-binding protein encoded by the region from 60.1 to 66.6 map units. The accumulation of cytoplasmic RNA sequences complementary to these l-strand genes under various conditions of infection and in certain lines of transformed cells has been investigated by solution hybridization of cytoplasmic RNA to the separated strands of restriction endonuclease fragments of adenoviral DNA. During the early phase, RNA sequences complementary to the region from 11.6 to 36.7 map units were present at a concentration of 10 to 60 copies per cell, regardless of the nature of the block used to inhibit viral DNA synthesis. By 24 h after infection in the absence of any such block, sequences complementary to the regions from 11.6 to 18.2 map units (IVa2) and from 18.6 to 36.7 map units (E2B) accumulated to concentrations of 4,800 and 280 copies per cell, respectively. The ratio of cytoplasmic E2A RNA sequences to E2B RNA sequences remained close to 10:1 throughout the time period investigated. Of the transformed cell lines which retained E2B DNA sequences that were examined, only the T2C4 line expressed these sequences in cytoplasmic RNA. The implications of these observations for regulation of expression of the adenoviral early l-strand genes are discussed.

Adenoviruses, Human↗
PubMed1980

Catalysis of adenovirus DNA synthesis in vitro by DNA polymerase gamma.

DNA replication complexes were purified from adenovirus type 5 (Ad5)-infected HeLa cells. DNA synthesis by these complexes in vitro was extremely sensitive to the inhibitors dideoxythymidine triphosphate, N-ethyl maleimide and p-hydroxymercuribenzoate. The bound DNA polymerase was released from the complexes by limited digestion with micrococcal nuclease. This released polymerase preferred poly(rA):(dT)12-18 as template over activated calf thymus DNA. These results are compatible with the major polymerase in the replication complex being of the gamma class.

Adenoviridae↗
PubMed1979

Characterization of two temperature-sensitive mutants of adenovirus type 5.

The properties of two temperature-sensitive mutants ts 18 and ts 19 of adenovirus type 5 were studied. It was demonstrated that they had a defect such that they failed to assemble virus and showed defective processing of infected cell polypeptides at the restrictive temperature. Analysis, after protease digestion, of the virions produced at the permissive temperature by SDS PAGE, and of the substrate availability of the mutants to the virus protein kinase suggested that polypeptide VI was defective in these mutants.

Adenoviruses, Human↗