Zobrazeno 1 - 10
of 12
pro vyhledávání: '"Christopher J. Woolstenhulme"'
Publikováno v:
Cell Reports, Vol 14, Iss 4, Pp 686-694 (2016)
The rate of protein synthesis varies according to the mRNA sequence in ways that affect gene expression. Global analysis of translational pausing is now possible with ribosome profiling. Here, we revisit an earlier report that Shine-Dalgarno sequence
Externí odkaz:
https://doaj.org/article/223274cd3c7547c0867397ade3c3d301
Publikováno v:
Cell Reports, Vol 11, Iss 1, Pp 13-21 (2015)
Ribosome profiling is a powerful method for globally assessing the activity of ribosomes in a cell. Despite its application in many organisms, ribosome profiling studies in bacteria have struggled to obtain the resolution necessary to precisely defin
Externí odkaz:
https://doaj.org/article/ecb7728168d248dc9a6ccf1c7c222dd3
Autor:
Agata L. Starosta, Jürgen Lassak, Lauri Peil, Gemma C. Atkinson, Christopher J. Woolstenhulme, Kai Virumäe, Allen Buskirk, Tanel Tenson, Jaanus Remme, Kirsten Jung, Daniel N. Wilson
Publikováno v:
Cell Reports, Vol 9, Iss 2, Pp 476-483 (2014)
Bacterial ribosomes stall on polyproline stretches and require the elongation factor P (EF-P) to relieve the arrest. Yet it remains unclear why evolution has favored the development of EF-P rather than selecting against the occurrence of polyproline
Externí odkaz:
https://doaj.org/article/23c5b8d5e45d445fb225503be0fc7649
Publikováno v:
Cell Reports, Vol 11, Iss 1, Pp 13-21 (2015)
SummaryRibosome profiling is a powerful method for globally assessing the activity of ribosomes in a cell. Despite its application in many organisms, ribosome profiling studies in bacteria have struggled to obtain the resolution necessary to precisel
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::afebe4b42cdfbbfa485ca9e01560bc57
https://doi.org/10.1016/j.celrep.2015.03.014
https://doi.org/10.1016/j.celrep.2015.03.014
Autor:
Preeti Saini, Thomas E. Dever, Allen R. Buskirk, Byung-Sik Shin, Joo-Ran Kim, Erik Gutierrez, Christopher J. Woolstenhulme
Publikováno v:
Molecular Cell. 51(1):35-45
Translation factor eIF5A, containing the unique amino acid hypusine, was originally shown to stimulate methionyl-puromycin synthesis, a model assay for peptide bond formation. More recently, eIF5A was shown to promote translation elongation; however,
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::3b0e073303c3bc4b30a1f39f702b5ae0
Publikováno v:
Cell Reports, Vol 14, Iss 4, Pp 686-694 (2016)
SummaryThe rate of protein synthesis varies according to the mRNA sequence in ways that affect gene expression. Global analysis of translational pausing is now possible with ribosome profiling. Here, we revisit an earlier report that Shine-Dalgarno s
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::34bcaa9ab4a82af2a4c8b0d1bf4959d5
https://pubmed.ncbi.nlm.nih.gov/26776510
https://pubmed.ncbi.nlm.nih.gov/26776510
Publikováno v:
Regulatory Nascent Polypeptides ISBN: 9784431550518
Although we tend to think that the ribosome can link together amino acids in any order, we have found that certain sequences interfere with protein synthesis. Characterization of stalling peptides found in bacteria has revealed multiple mechanisms of
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::119971e31b3ceaebd8603af4ea3bb9be
https://doi.org/10.1007/978-4-431-55052-5_13
https://doi.org/10.1007/978-4-431-55052-5_13
Autor:
Kirsten Jung, Gemma C. Atkinson, Kai Virumäe, Tanel Tenson, Christopher J. Woolstenhulme, Jaanus Remme, Daniel N. Wilson, Agata L. Starosta, Jürgen Lassak, Lauri Peil, Allen R. Buskirk
Publikováno v:
Cell Reports, Vol 9, Iss 2, Pp 476-483 (2014)
SummaryBacterial ribosomes stall on polyproline stretches and require the elongation factor P (EF-P) to relieve the arrest. Yet it remains unclear why evolution has favored the development of EF-P rather than selecting against the occurrence of polyp
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::82c39c6e9661b9e1e65dafb80d6cfabb
http://urn.kb.se/resolve?urn=urn:nbn:se:umu:diva-97232
http://urn.kb.se/resolve?urn=urn:nbn:se:umu:diva-97232
Autor:
E. Nicholas Petersen, Shankar Parajuli, David Healey, W. Evan Johnson, Nicholas R. Guydosh, Allen R. Buskirk, Christopher J. Woolstenhulme, Daniel N. Wilson, Diana P. Valverde, Agata L. Starosta
Publikováno v:
Proceedings of the National Academy of Sciences. 110
Although the ribosome is a very general catalyst, it cannot synthesize all protein sequences equally well. For example, ribosomes stall on the secretion monitor (SecM) leader peptide to regulate expression of a downstream gene. Using a genetic select
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::a29c2bb27aab24d2921d3bd1368391a4
https://doi.org/10.1073/pnas.1219536110
https://doi.org/10.1073/pnas.1219536110
Publikováno v:
Ribosomes ISBN: 9783709102145
Not all translation reactions end in the synthesis of a full-length protein. In bacteria, ribosomes stall at the 3′ end of mRNA transcripts lacking stop codons, as they cannot efficiently employ release factors for termination and recycling. Some n
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::b811955c6e56e9e14bf51b5eb987124b
https://doi.org/10.1007/978-3-7091-0215-2_29
https://doi.org/10.1007/978-3-7091-0215-2_29