Zobrazeno 1 - 7
of 7
pro vyhledávání: '"Stephen M. Garrey"'
Autor:
Stephen M. Garrey, George A. Mackie
Publikováno v:
Molecular Microbiology. 80:1613-1624
Viable mutations affecting the 5'-phosphate sensor of RNase E, including R169Q or T170A, become lethal when combined with deletions removing part of the non-catalytic C-terminal domain of RNase E. The phosphate sensor is required for efficient autore
Autor:
Stephen M. Garrey, Jenna L. Riffell, Janet S. Hankins, Ying-Han Roger Hsu, George A. Mackie, Melinda M. Diver, Michaela Blech, Vitharani Kunanithy, Leigh M. Stickney
Publikováno v:
Journal of Biological Chemistry. 284:31843-31850
The paralogous endoribonucleases, RNase E and RNase G, play major roles in intracellular RNA metabolism in Escherichia coli and related organisms. To assay the relative importance of the principal RNA binding sites identified by crystallographic anal
Publikováno v:
RNA. 14:78-88
In yeast (Saccharoymces cerevisiae), the branchpoint binding protein (BBP) recognizes the conserved yeast branchpoint sequence (UACUAAC) with a high level of specificity and affinity, while the human branchpoint binding protein (SF1) binds the less-c
Autor:
Kerri York, Stanley Fields, Mantas Prekeris, Adam Katolik, Sarah S. Bernards, Jay R. Hesselberth, Xueni Li, Stephen M. Garrey, Masad J. Damha, Rui Zhao
Turnover of the branched RNA intermediates and products of pre-mRNA splicing is mediated by the lariat-debranching enzyme Dbr1. We characterized a homolog of Dbr1 from Saccharomyces cerevisiae, Drn1/Ygr093w, that has a pseudo-metallophosphodiesterase
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::64edfa5e0c4b14d376f731daa5f5b036
https://europepmc.org/articles/PMC4105757/
https://europepmc.org/articles/PMC4105757/
Autor:
Stephen M, Garrey, George A, Mackie
Publikováno v:
Molecular microbiology. 80(6)
Viable mutations affecting the 5'-phosphate sensor of RNase E, including R169Q or T170A, become lethal when combined with deletions removing part of the non-catalytic C-terminal domain of RNase E. The phosphate sensor is required for efficient autore
Autor:
Stephen M, Garrey, Michaela, Blech, Jenna L, Riffell, Janet S, Hankins, Leigh M, Stickney, Melinda, Diver, Ying-Han Roger, Hsu, Vitharani, Kunanithy, George A, Mackie
Publikováno v:
The Journal of biological chemistry. 284(46)
The paralogous endoribonucleases, RNase E and RNase G, play major roles in intracellular RNA metabolism in Escherichia coli and related organisms. To assay the relative importance of the principal RNA binding sites identified by crystallographic anal
Publikováno v:
The Journal of biological chemistry. 281(37)
The highly conserved branch point sequence (BPS) of UACUAAC in Saccharomyces cerevisiae is initially recognized by the branch point-binding protein (BBP). Using systematic evolution of ligands by exponential enrichment we have determined that yeast B