Zobrazeno 1 - 10
of 51
pro vyhledávání: '"Martin R. Boocock"'
Autor:
Gillian M. Cadden, Jan-Gero Schloetel, Grant McKenzie, Martin R. Boocock, Steven W. Magennis, W. Marshall Stark
Publikováno v:
Nature Communications, Vol 15, Iss 1, Pp 1-14 (2024)
Abstract Serine recombinases are proposed to catalyse site-specific recombination by a unique mechanism called subunit rotation. Cutting and rejoining DNA occurs within an intermediate synaptic complex comprising a recombinase tetramer bound to two D
Externí odkaz:
https://doaj.org/article/a5af090df6ae4a95ae5b44f9a56f251c
Autor:
Sherwin P Montaño, Sally-J Rowland, James R Fuller, Mary E Burke, Alasdair I MacDonald, Martin R Boocock, W Marshall Stark, Phoebe A Rice
Publikováno v:
Nucleic acids research.
Site-specific DNA recombinases play a variety of biological roles, often related to the dissemination of antibiotic resistance, and are also useful synthetic biology tools. The simplest site-specific recombination systems will recombine any two cogna
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::a238aff985a0bf14f39d3d367d29b490
https://pubmed.ncbi.nlm.nih.gov/36100255
https://pubmed.ncbi.nlm.nih.gov/36100255
Publikováno v:
Molecular Microbiology. 114:952-965
The site-specific recombinase Tn3 resolvase initiates DNA strand exchange when two res recombination sites and six resolvase dimers interact to form a synapse. The detailed architecture of this intricate recombination machine remains unclear. We have
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::66fad640d81e478e9e8b1f0ce25521aa
https://doi.org/10.1111/mmi.14579
https://doi.org/10.1111/mmi.14579
Publikováno v:
Nucleic Acids Research
Members of the serine family of site-specific recombinases exchange DNA strands via 180° rotation about a central protein-protein interface. Modeling of this process has been hampered by the lack of structures in more than one rotational state for a
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::5a2f5536aec557c144f2fd6585346340
https://pubmed.ncbi.nlm.nih.gov/29315406
https://pubmed.ncbi.nlm.nih.gov/29315406
Publikováno v:
Acta Crystallographica Section A Foundations and Advances. 75:a28-a28
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::8675aa4e62c76242550d6d651bbdf154
https://doi.org/10.1107/s0108767319099719
https://doi.org/10.1107/s0108767319099719
Autor:
Phoebe A. Rice, Robert S. Daum, Agnieszka Misiura, Susan Boyle-Vavra, Ying Z. Pigli, Martin R. Boocock
Publikováno v:
Molecular Microbiology. 88:1218-1229
Methicillin-resistant Staphylococcus aureus (MRSA) emerged via acquisition of a mobile element, staphylococcal cassette chromosome mec (SCCmec). Integration and excision of SCCmec is mediated by an unusual site-specific recombination system. Most var
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::77a41ac0002c175bd826b241b39f8b2d
https://doi.org/10.1111/mmi.12253
https://doi.org/10.1111/mmi.12253
Publikováno v:
Structure. 19:799-809
SummarySin resolvase is a site-specific serine recombinase that is normally controlled by a complex regulatory mechanism. A single mutation, Q115R, allows the enzyme to bypass the entire regulatory apparatus, such that no accessory proteins or DNA si
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::243f5e980958ec84aad128b2f76c993a
https://doi.org/10.1016/j.str.2011.03.017
https://doi.org/10.1016/j.str.2011.03.017
Autor:
Sally-J. Rowland, Nan-Sheng Li, Joseph A. Piccirilli, Andrew M. Steiner, Rodolfo Ghirlando, W. Marshall Stark, Martin R. Boocock, Phoebe A. Rice, Kent W. Mouw
Publikováno v:
Journal of Molecular Biology. 404:16-33
Serine recombinases promote specific DNA rearrangements by a "cut and paste" mechanism which involves cleavage of all four DNA strands at two sites recognized by the enzyme. Dissecting the order and timing of these cleavage events and the steps leadi
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::4b4637897965a0864841a428ea9f7594
https://doi.org/10.1016/j.jmb.2010.08.057
https://doi.org/10.1016/j.jmb.2010.08.057
Autor:
Sherwin P. Montaño, Phoebe A. Rice, Kent W. Mouw, Sally J. Rowland, W. Marshall Stark, Martin R. Boocock
Publikováno v:
Biochemical Society Transactions. 38:384-387
A remarkable feature of the serine resolvases is their regulation: the wild-type enzymes will catalyse intra- but not inter-molecular recombination, can sense the relative orientation of their sites and can exchange strands directionally, despite the
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::eb1ffb9426fceaf728691e5a108bc299
https://doi.org/10.1042/bst0380384
https://doi.org/10.1042/bst0380384
Autor:
Sally-J. Rowland, W. Marshall Stark, Arlene L. McPherson, Martin R. Boocock, Phoebe A. Rice, Kent W. Mouw
Publikováno v:
Molecular Microbiology
The resolvase Sin regulates DNA strand exchange by assembling an elaborate interwound synaptosome containing catalytic and regulatory Sin tetramers, and an architectural DNA-bending protein. The crystal structure of the regulatory tetramer was recent
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::8c0b43d439bda3df988b3d2fc9273b54
http://europepmc.org/articles/PMC2764113
http://europepmc.org/articles/PMC2764113