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The Rate-Determining Step on the recA Protein-Catalyzed ssDNA-Dependent ATP Hydrolysis Reaction Pathway

Publikováno v: Biochemistry. 36:3483-3490

We recently constructed a mutant recA protein in which His 163 was replaced by a tryptophan residue. The [H163W]recA protein is functionally identical to the wild-type protein, and the Trp163 side chain serves as a fluorescence reporter group for the

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::3a08f5686210feae0cd900708f80cbd8
https://doi.org/10.1021/bi962881l

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Introduction of a tryptophan reporter group into loop 1 of the recA protein. Examination of the conformational states of the recA-ssDNA complex by fluorescence spectroscopy

Autor: Einar Stole, Floyd R. Bryant

Publikováno v: Journal of Biological Chemistry. 269:7919-7925

Site-directed mutagenesis was used to replace His-163 in the Loop 1 region of the recA protein with a tryptophan residue. The [H163W]recA protein binds single-stranded DNA (ssDNA), catalyzes ssDNA-dependent ATP hydrolysis, and is fully active in the

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_________::17373084f7cf50e10a76f9dc7bd1b19d
https://doi.org/10.1016/s0021-9258(17)37139-9

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Inhibition of glutathione synthesis in the newborn rat: a model for endogenously produced oxidative stress

Autor: Ajey Jain, Alton Meister, William W. Frayer, Peter A. M. Auld, Einar Stole, Johannes Martensson

Publikováno v: Proceedings of the National Academy of Sciences. 88:9360-9364

A model for oxidative stress is described in which glutathione (GSH) synthesis is selectively blocked in newborn rats by administration of L-buthionine-(S,R)-sulfoximine (BSO). In this model, the normal endogenous physiological formation of reactive

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::aaa21205cb1a7f5a67c8d1fb9d28ed85
https://doi.org/10.1073/pnas.88.20.9360

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Identification of a highly reactive threonine residue at the active site of gamma-glutamyl transpeptidase

Autor: Daniel Wellner, Alton Meister, Andrew P. Seddon, Einar Stole

Publikováno v: Proceedings of the National Academy of Sciences. 87:1706-1709

gamma-Glutamyl transpeptidase [(5-glutamyl)-peptide:amino-acid 5-glutamyltransferase, EC 2.3.2.2], an enzyme of major importance in glutathione metabolism, was inactivated by treating it with L-(alpha S,5S)-alpha-amino-3-chloro-4,5-dihydro-5-[3-14C]i

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::73954a666dd1e1b357491b79cc0a2700
https://doi.org/10.1073/pnas.87.5.1706

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Reengineering the nucleotide cofactor specificity of the RecA protein by mutation of aspartic acid 100

Autor: Einar Stole, Floyd R. Bryant

Publikováno v: The Journal of biological chemistry. 271(31)

We have recently obtained evidence for a direct linkage between the S0.5 (S0.5 is the substrate concentration required for half-maximal velocity) value of a nucleoside triphosphate and the conformational state of the RecA-ssDNA complex, with an S0.5

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::0d1214817a58925d6b5a45915255bdc4
https://pubmed.ncbi.nlm.nih.gov/8702471

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Spectroscopic demonstration of a linkage between the kinetics of NTP hydrolysis and the conformational state of the recA-single-stranded DNA complex

Autor: Floyd R. Bryant, Einar Stole

Publikováno v: The Journal of biological chemistry. 270(35)

We recently constructed a mutant recA protein in which His-163 was replaced by a tryptophan residue; the [H163W]recA protein is functionally identical to the wild-type protein, and the Trp-163 side chain serves as a reporter group for the conformatio

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::eff4542a6aeeacf2a76ea18ca1cb9ccf
https://pubmed.ncbi.nlm.nih.gov/7657604

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