Zobrazeno 1 - 10
of 218
pro vyhledávání: '"Joseph D Puglisi"'
Publikováno v:
eLife, Vol 3 (2014)
The signal recognition particle (SRP) directs translating ribosome-nascent chain complexes (RNCs) that display a signal sequence to protein translocation channels in target membranes. All previous work on the initial step of the targeting reaction, w
Externí odkaz:
https://doaj.org/article/a7253254f1e642608187cb2d1624ed36
Autor:
Jinfan Wang, Jing Wang, Byung-Sik Shin, Joo-Ran Kim, Thomas E. Dever, Joseph D. Puglisi, Israel S. Fernández
Publikováno v:
Nature Communications, Vol 11, Iss 1, Pp 1-8 (2020)
The GTPase eIF5B is involved in the correct positioning of the initiator Met-tRNAi Me t on the ribosome during the late stages of translation initiation. Here the authors present a cryo-EM structure of the ribosome in complex with eIF5B and Met-tRNAi
Externí odkaz:
https://doaj.org/article/c83cad0e29c9428c8c5db019de2b15ba
Autor:
Manasvi Verma, Junhong Choi, Kyle A. Cottrell, Zeno Lavagnino, Erica N. Thomas, Slavica Pavlovic-Djuranovic, Pawel Szczesny, David W. Piston, Hani S. Zaher, Joseph D. Puglisi, Sergej Djuranovic
Publikováno v:
Nature Communications, Vol 10, Iss 1, Pp 1-15 (2019)
Several factors contribute to the efficiency of protein expression. Here the authors show that the identity of amino acids encoded by codons at position 3–5 significantly impact translation efficiency and protein expression levels.
Externí odkaz:
https://doaj.org/article/d6c7739bcd3d4753818faecc0bc65dc2
Autor:
Olivier Duss, Galina A. Stepanyuk, Annette Grot, Seán E. O’Leary, Joseph D. Puglisi, James R. Williamson
Publikováno v:
Nature Communications, Vol 9, Iss 1, Pp 1-14 (2018)
The early steps of ribosome assembly occur co-transcriptionally on the nascent ribosomal RNA. Here the authors demonstrate an approach that allows simultaneous monitoring of transcription and ribosomal protein assembly at the single-molecule level in
Externí odkaz:
https://doaj.org/article/0fe00cc7c750481fa2a7c9346d042e43
Publikováno v:
Cell Reports, Vol 20, Iss 1, Pp 161-172 (2017)
During termination of translation, the nascent peptide is first released from the ribosome, which must be subsequently disassembled into subunits in a process known as ribosome recycling. In bacteria, termination and recycling are mediated by the tra
Externí odkaz:
https://doaj.org/article/ab72c6d010b348fa89bd159ed0022a4c
Autor:
Christopher P. Lapointe, Rosslyn Grosely, Masaaki Sokabe, Carlos Alvarado, Jinfan Wang, Elizabeth Montabana, Nancy Villa, Byung-Sik Shin, Thomas E. Dever, Christopher S. Fraser, Israel S. Fernández, Joseph D. Puglisi
Publikováno v:
Nature, vol 607, iss 7917
Nature
Nature
Translation initiation defines the identity and quantity of a synthesized protein. The process is dysregulated in many human diseases1,2. A key commitment step is when the ribosomal subunits join at a translation start site on a messenger RNA to form
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::cf2eaa553481dbec6647d6a7bc376aca
https://doi.org/10.1038/s41586-022-04858-z
https://doi.org/10.1038/s41586-022-04858-z
Autor:
Arjun Prabhakar, Michael Y Pavlov, Jingji Zhang, Gabriele Indrisiunaite, Jinfan Wang, Michael R Lawson, Måns Ehrenberg, Joseph D Puglisi
Publikováno v:
Nucleic Acids Research.
In bacteria, release of newly synthesized proteins from ribosomes during translation termination is catalyzed by class-I release factors (RFs) RF1 or RF2, reading UAA and UAG or UAA and UGA codons, respectively. Class-I RFs are recycled from the post
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::c647bc9fc49791aeda26ff75433708b5
https://doi.org/10.1093/nar/gkad286
https://doi.org/10.1093/nar/gkad286
Autor:
Ola B. Nilsson, Rickard Hedman, Jacopo Marino, Stephan Wickles, Lukas Bischoff, Magnus Johansson, Annika Müller-Lucks, Fabio Trovato, Joseph D. Puglisi, Edward P. O’Brien, Roland Beckmann, Gunnar von Heijne
Publikováno v:
Cell Reports, Vol 12, Iss 10, Pp 1533-1540 (2015)
At what point during translation do proteins fold? It is well established that proteins can fold cotranslationally outside the ribosome exit tunnel, whereas studies of folding inside the exit tunnel have so far detected only the formation of helical
Externí odkaz:
https://doaj.org/article/be6170e22afe4e52a52d732392b7ce19
Publikováno v:
Cell Reports, Vol 7, Iss 5, Pp 1534-1546 (2014)
The traditional view of macrolide antibiotics as plugs inside the ribosomal nascent peptide exit tunnel (NPET) has lately been challenged in favor of a more complex, heterogeneous mechanism, where drug-peptide interactions determine the fate of a tra
Externí odkaz:
https://doaj.org/article/6b77b6f67b57460b98af1604488636da