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Interaction of the bacteriophage T4 gene 59 helicase loading protein and gene 41 helicase with each other and with fork, flap, and cruciform DNA

Autor: C E, Jones, T C, Mueser, N G, Nossal

Publikováno v: The Journal of biological chemistry. 275(35)

Bacteriophage T4 gene 59 helicase loading protein accelerates the loading of T4 gene 41 DNA helicase and is required for recombination-dependent DNA replication late in T4 phage infection. The crystal structure of 59 protein revealed a two-domain alp

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=pmid________::00cd3e9a3c58a1c47b0534b9d7abdcd0
https://pubmed.ncbi.nlm.nih.gov/10871615

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Bacteriophage T4 gene 59 helicase assembly protein binds replication fork DNA. The 1.45 A resolution crystal structure reveals a novel alpha-helical two-domain fold

Autor: T C, Mueser, C E, Jones, N G, Nossal, C C, Hyde

Publikováno v: Journal of molecular biology. 296(2)

The bacteriophage T4 gene 59 helicase assembly protein is required for recombination-dependent DNA replication, which is the predominant mode of DNA replication in the late stage of T4 infection. T4 gene 59 helicase assembly protein accelerates the l

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=pmid________::a556f5a68962e294c024003685e74a99
https://pubmed.ncbi.nlm.nih.gov/10669611

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Either bacteriophage T4 RNase H or Escherichia coli DNA polymerase I is essential for phage replication

Autor: N G Nossal, L J Hobbs

Bacteriophage T4 rnh encodes an RNase H that removes ribopentamer primers from nascent DNA chains during synthesis by the T4 multienzyme replication system in vitro (H. C. Hollingsworth and N. G. Nossal, J. Biol. Chem. 266:1888-1897, 1991). This pape

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::9161dc1e4fbd61c79714e63afc241eaa
https://europepmc.org/articles/PMC178574/

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Purification of bacteriophage T4 DNA replication proteins

Autor: N G, Nossal, D M, Hinton, L J, Hobbs, P, Spacciapoli

Publikováno v: Methods in enzymology. 262

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=pmid________::981148a4eaab4ca579397163b8c71a3e
https://pubmed.ncbi.nlm.nih.gov/8594379

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Interaction of DNA polymerase and DNA helicase within the bacteriophage T4 DNA replication complex. Leading strand synthesis by the T4 DNA polymerase mutant A737V (tsL141) requires the T4 gene 59 helicase assembly protein

Autor: P, Spacciapoli, N G, Nossal

Publikováno v: The Journal of biological chemistry. 269(1)

The bacteriophage T4 tsL141 (A737V) mutant in T4 DNA polymerase is temperature-sensitive for DNA replication and an antimutator for some types of mutations. In the accompanying paper (Spacciapoli, P., and Nossal, N. G. (1993) J. Biol. Chem. 269, 438-

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=pmid________::049e194b8224115519d15ebf1621a34a
https://pubmed.ncbi.nlm.nih.gov/8276834

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A single mutation in bacteriophage T4 DNA polymerase (A737V, tsL141) decreases its processivity as a polymerase and increases its processivity as a 3'--5' exonuclease

Autor: P, Spacciapoli, N G, Nossal

Publikováno v: The Journal of biological chemistry. 269(1)

The bacteriophage T4 DNA polymerase mutant A737V (tsL141 and tsCB120) was originally characterized as temperature-sensitive for DNA replication and an antimutator for transition mutations. Its antimutator phenotype is suppressed by the L771F mutation

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=pmid________::8258402fa0bd4668f843bba5002c707a
https://pubmed.ncbi.nlm.nih.gov/8276833

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Bacteriophage T4 encodes an RNase H which removes RNA primers made by the T4 DNA replication system in vitro

Autor: H C, Hollingsworth, N G, Nossal

Publikováno v: The Journal of biological chemistry. 266(3)

RNase H activity increases markedly after bacteriophage T4 infection of Escherichia coli MIC2003, an RNase H-deficient host. We have extensively purified the RNase H from these T4-infected cells and have shown that the RNase H activity copurifies wit

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=pmid________::1e96665a93e8fe5355a7dbdb0750d88c
https://pubmed.ncbi.nlm.nih.gov/1703156

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Bacteriophage T4 DNA primase-helicase. Characterization of the DNA synthesis primed by T4 61 protein in the absence of T4 41 protein

Autor: N G Nossal, D M Hinton

Publikováno v: Journal of Biological Chemistry. 262:10879-10885

The bacteriophage T4 61/41 protein primase-helicase is part of a seven T4 protein system needed for DNA synthesis in vitro. Although both 41 and 61 proteins are required for the synthesis and utilization of the normal pppApC(pN)3 pentanucleotide prim

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_________::067658ef8150cc63f42f38d544e2ecae
https://doi.org/10.1016/s0021-9258(18)61046-4

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DNA replication by bacteriophage T4 proteins. The T4 43, 32, 44–62, And 45 proteins are required for strand displacement synthesis at nicks in duplex DNA

Autor: B M Peterlin, N G Nossal

Publikováno v: Journal of Biological Chemistry. 254:6032-6037

The T4 bacteriophage gene 43 (T4 DNA polymerase), 32 (DNA helix-destabilizing protein), and 45 proteins and the complex of the gene 44 and 62 proteins are all required for DNA synthesis beginning at single-stranded breaks in duplex DNA. This synthesi

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_________::98ef38c0229b6fc0b49076f19a71e08e
https://doi.org/10.1016/s0021-9258(18)50515-9

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Bacteriophage T4 DNA primase-helicase. Characterization of oligomer synthesis by T4 61 protein alone and in conjunction with T4 41 protein

Autor: D M Hinton, N G Nossal

Publikováno v: Journal of Biological Chemistry. 262:10873-10878

The bacteriophage T4 41 and 61 proteins function as a primase-helicase which in vitro both unwinds double-stranded DNA and synthesizes the pentaribonucleotides used to initiate DNA synthesis on the lagging strand. We demonstrate that 61 protein alone

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_________::893d57f1719d05950cf9cf68278cb565
https://doi.org/10.1016/s0021-9258(18)61045-2

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