Výsledky vyhledávání - "G. N. Godson"

Interaction of Escherichia coli primase with a phage G4ori(c)-E. coli SSB complex

Autor: Wuliang Sun, G N Godson

Publikováno v: Journal of Bacteriology. 178:6701-6705

We earlier reported that Escherichia coli single-stranded DNA-binding protein (SSB) bound in a fixed position to the stem-loop structure of the origin of complementary DNA strand synthesis in phage G4 (G4ori(c)), leaving stem-loop I and the adjacent

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::6478e4e7f61ad4781e9bd541fdbd13f0
https://doi.org/10.1128/jb.178.23.6701-6705.1996

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ATP Cross-Linked to Escherichia coli Single-Strand DNA-Binding Protein Can Be Utilized by the Catalytic Center of Primase as Initiating Nucleotide for Primer RNA Synthesis on Phage G4oric Template

Autor: Wuliang Sun, G N Godson, A. A. Mustaev

Publikováno v: Biochemistry. 37:3810-3817

We report a new observation of the role of Escherichia coli single-strand DNA binding protein (SSB) in synthesis of primer RNA (pRNA) catalyzed by.E.coli primase on the SSB-coated phage G4oric template. Using a set of ATP priming substrates with reac

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https://doi.org/10.1021/bi972455f

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Selective decay of Escherichia coli dnaG messenger RNA is initiated by RNase E

Autor: G. N. Godson, Vijay Yajnik

Publikováno v: Journal of Biological Chemistry. 268:13253-13260

The rpsU-dnaG-rpoD operon messenger RNA that encodes S21, primase, and sigma-70 is cleaved under normal physiological conditions. The dnaG coding portion of the mRNA is then rapidly degraded. An endonuclease activity has been isolated from wild type

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_________::e4a86ee40b42dca00b5dc2ce978f7968
https://doi.org/10.1016/s0021-9258(19)38645-4

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Binding and phasing of Escherichia coli single-stranded DNA-binding protein by the secondary structure of phage G4 origin of complementary DNA strand synthesis (G4oric)

Autor: G. N. Godson, Wuliang Sun

Publikováno v: Journal of Biological Chemistry. 268:8026-8039

The origin of phage G4 DNA complementary strand synthesis (G4oric) consists of three stem-loop structures (stem loops I, II, and III) that have been proposed as a recognition site for primase during primer RNA (pRNA) synthesis (Godson, G. N., Barrell

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_________::02a6cbaab102aceb7c2123c3e616b573
https://doi.org/10.1016/s0021-9258(18)53059-3

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Cloning and nucleotide sequence of a chromosomally encoded tetracycline resistance determinant, tetA(M), from a pathogenic, methicillin-resistant strain of Staphylococcus aureus

Autor: P. Svec, M Nesin, B Kreiswirth, J Kornblum, J R Lupski, S J Projan, G N Godson

Publikováno v: Antimicrobial Agents and Chemotherapy. 34:2273-2276

This report describes the cloning and sequencing of a chromosomally encoded tetracycline resistance determinant from a clinical isolate of methicillin-resistant Staphylococcus aureus. On the basis of the sequence, the gene is in the tet(M) class, and

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https://doi.org/10.1128/aac.34.11.2273

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Identification of the magnesium ion binding site in the catalytic center of Escherichia coli primase by iron cleavage

Autor: Wuliang Sun, A. A. Mustaev, G N Godson, Schoenich J

Publikováno v: Biochemistry. 39(2)

Magnesium is essential for the catalysis reaction of Escherichia coli primase, the enzyme synthesizing primer RNA chains for initiation of DNA replication. To map the Mg(2+) binding site in the catalytic center of primase, we have employed the iron c

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https://pubmed.ncbi.nlm.nih.gov/10630993

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Biochemical characterization of Escherichia coli temperature-sensitive dnaB mutants dnaB8, dnaB252, dnaB70, dnaB43, and dnaB454

Autor: D Saluja, G N Godson

By use of PCR, the dnaB genes from the classical temperature-sensitive dnaB mutants PC8 (dnaB8), RS162 (dnaB252), CR34/454 (dnaB454), HfrH165/70 (dnaB70), and CR34/43 (dnaB43) were isolated. The mutant genes were sequenced, and single amino acid chan

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::1f9876083f4b849206d6f868ee347f9e
https://europepmc.org/articles/PMC176710/

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Domains of Escherichia coli primase: functional activity of a 47-kDa N-terminal proteolytic fragment

Autor: J. Tormo, T. A. Steitz, G. N. Godson, Wuliang Sun

Endoproteinase Asp-N cleaves the 581-amino acid Escherichia coli primase (65,564 Da) into several major fragments. One of these, a 47-kDa fragment containing the complete N terminus and the first 422 amino acids of primase, is capable of primer RNA (

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::17568feb921863030e49f96b386e504f
https://europepmc.org/articles/PMC45251/

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