Zobrazeno 1 - 10
of 20
pro vyhledávání: '"Margaret M. Suhanovsky"'
Autor:
Christiane Brugger, Cheng Zhang, Margaret M. Suhanovsky, David D. Kim, Amy N. Sinclair, Dmitry Lyumkis, Alexandra M. Deaconescu
Publikováno v:
Nature Communications, Vol 11, Iss 1, Pp 1-12 (2020)
Transcription-repair coupling factors (TRCFs) are large ATPases that mediate the preferential repair of the transcribed DNA strand. Here the authors reveal the cryo-EM structure of DNA-bound Mfd, the bacterial TRCF, and provide molecular insights int
Externí odkaz:
https://doaj.org/article/49f049022732482596be8740194b4dd5
Autor:
Christiane Brugger, Alexandra M. Deaconescu, Margaret M. Suhanovsky, Arti Tripathi, Song Tong, Amita Sastry, Joel R. Hoskins, Victoria Dorich, Susan Gottesman, Sue Wickner
Publikováno v:
Genes & Development. 33:718-732
The stationary phase promoter specificity subunit σS (RpoS) is delivered to the ClpXP machinery for degradation dependent on the adaptor RssB. This adaptor-specific degradation of σS provides a major point for regulation and transcriptional reprogr
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::a20243b6af5087d6c7bf07b643f2a9e2
https://doi.org/10.1101/gad.320168.118
https://doi.org/10.1101/gad.320168.118
Autor:
Margaret M. Suhanovsky, Cheng Zhang, Alexandra M. Deaconescu, Amy N. Sinclair, Dmitry Lyumkis, David D. Kim, Christiane Brugger
Publikováno v:
Nature Communications
Nature Communications, Vol 11, Iss 1, Pp 1-12 (2020)
Nature Communications, Vol 11, Iss 1, Pp 1-12 (2020)
Mfd couples transcription to nucleotide excision repair, and acts on RNA polymerases when elongation is impeded. Depending on impediment severity, this action results in either transcription termination or elongation rescue, which rely on ATP-depende
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::f73994e9bf86cf0c22f635ec544438fc
https://doi.org/10.1038/s41467-020-17457-1
https://doi.org/10.1038/s41467-020-17457-1
Publikováno v:
Photochemistry and Photobiology. 93:268-279
Photochemical and other reactions on DNA cause damage and corrupt genetic information. To counteract this damage, organisms have evolved intricate repair mechanisms that often crosstalk with other DNA-based processes, such as transcription. Intriguin
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::832cc2e8df2d32d1440bac599670f2b1
https://doi.org/10.1111/php.12661
https://doi.org/10.1111/php.12661
Publikováno v:
Virology. :487-497
For many (if not all) bacterial and archaeal tailed viruses and eukaryotic Herpesvirdae the HK97-fold serves as the major architectural element in icosahedral capsid formation while still enabling the conformational flexibility required during assemb
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::f403c9dea1ab8ff6c054c5ae112fcdd7
Autor:
LaTasha C.R. Fraser, Margaret M. Suhanovsky, Matthew L. Baker, Carolyn M. Teschke, Michael L. Gross, Wah Chiu, Don L. Rempel, Lisa M. Jones, Andrei T. Alexandrescu, Alessandro A. Rizzo
Publikováno v:
Structure. 22(6):830-841
Summary Some capsid proteins built on the ubiquitous HK97-fold have accessory domains imparting specific functions. Bacteriophage P22 coat protein has a unique insertion domain (I-domain). Two prior I-domain models from subnanometer cryoelectron micr
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::40989de8428f140c195043ff32d295a9
Autor:
LaTasha C.R. Fraser, Margaret M. Suhanovsky, Carolyn M. Teschke, Sarah R. Sheftic, Alessandro A. Rizzo, Andrei T. Alexandrescu
Publikováno v:
Biomolecular NMR Assignments. 7:257-260
The bacteriophage P22 virion is assembled from identical coat protein monomers in a complex reaction that is generally conserved among tailed, double-stranded DNA bacteriophages and viruses. Many coat proteins of dsDNA viruses have structures based o
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::77ca299d21b27c98e3e7669f2a8e9703
https://doi.org/10.1007/s12104-012-9422-x
https://doi.org/10.1007/s12104-012-9422-x
Publikováno v:
Virology. 428:64-69
In vitro assembly of bacteriophage P22 procapsids requires coat protein and sub-stoichiometric concentrations of the internal scaffolding protein. If there is no scaffolding protein, coat protein assembles aberrantly, but only at higher concentration
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::44fd02f99a20bd3f440fb9d67bf855ca
https://doi.org/10.1016/j.virol.2012.03.017
https://doi.org/10.1016/j.virol.2012.03.017
Autor:
Kristin N. Parent, Margaret M. Suhanovsky, Timothy S. Baker, Sarah E. Dunn, Carolyn M. Teschke
Publikováno v:
Molecular Microbiology. 77:1568-1582
Summary We have investigated determinants of polyhead for- mation in bacteriophage P22 in order to understand the molecular mechanism by which coat protein assembly goes astray. Polyhead assembly is caused by amino acid substitutions in coat protein
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::b68b0696fd00d518fd5cfb633e3e7ce2
https://doi.org/10.1111/j.1365-2958.2010.07311.x
https://doi.org/10.1111/j.1365-2958.2010.07311.x
Autor:
Susan Gottesman, Joel R. Hoskins, Arti Tripathi, Margaret M. Suhanovsky, Sue Wickner, Song Tong, Alexandra M. Deaconescu, Christiane Brugger, Victoria Dorich
Publikováno v:
Acta Crystallographica Section A Foundations and Advances. 74:e44-e44
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::b1c518f8ae11fe09e87b55127b5bc972
https://doi.org/10.1107/s2053273318094548
https://doi.org/10.1107/s2053273318094548