Zobrazeno 1 - 10
of 242
pro vyhledávání: '"Irmgard Sinning"'
Publikováno v:
Nature Communications, Vol 15, Iss 1, Pp 1-11 (2024)
Abstract Nascent chains undergo co-translational enzymatic processing as soon as their N-terminus becomes accessible at the ribosomal polypeptide tunnel exit (PTE). In eukaryotes, N-terminal methionine excision (NME) by Methionine Aminopeptidases (MA
Externí odkaz:
https://doaj.org/article/0123eb61d7f24baba7203f110d4065f4
Publikováno v:
Nature Communications, Vol 15, Iss 1, Pp 1-10 (2024)
Abstract Excision of the initiator methionine is among the first co-translational processes that occur at the ribosome. While this crucial step in protein maturation is executed by two types of methionine aminopeptidases in eukaryotes (MAP1 and MAP2)
Externí odkaz:
https://doaj.org/article/b3ca6428a47744678403641cb179afb2
Autor:
Melanie A. McDowell, Michael Heimes, Giray Enkavi, Ákos Farkas, Daniel Saar, Klemens Wild, Blanche Schwappach, Ilpo Vattulainen, Irmgard Sinning
Publikováno v:
Nature Communications, Vol 14, Iss 1, Pp 1-16 (2023)
Abstract The eukaryotic guided entry of tail-anchored proteins (GET) pathway mediates the biogenesis of tail-anchored (TA) membrane proteins at the endoplasmic reticulum. In the cytosol, the Get3 chaperone captures the TA protein substrate and delive
Externí odkaz:
https://doaj.org/article/b6447c79d60b44f2a61ff200ac48153d
Autor:
Valentin Bohl, Nele Merret Hollmann, Tobias Melzer, Panagiotis Katikaridis, Lena Meins, Bernd Simon, Dirk Flemming, Irmgard Sinning, Janosch Hennig, Axel Mogk
Publikováno v:
eLife, Vol 12 (2024)
Heat stress can cause cell death by triggering the aggregation of essential proteins. In bacteria, aggregated proteins are rescued by the canonical Hsp70/AAA+ (ClpB) bi-chaperone disaggregase. Man-made, severe stress conditions applied during, e.g.,
Externí odkaz:
https://doaj.org/article/f1f84471eab94033a5c0219bacf5ae11
Autor:
Xiaodi Gong, Jean-Baptiste Boyer, Simone Gierlich, Marlena Pożoga, Jonas Weidenhausen, Irmgard Sinning, Thierry Meinnel, Carmela Giglione, Yonghong Wang, Rüdiger Hell, Markus Wirtz
Publikováno v:
Cell Reports, Vol 43, Iss 2, Pp 113768- (2024)
Summary: The ribosome-tethered N-terminal acetyltransferase A (NatA) acetylates 52% of soluble proteins in Arabidopsis thaliana. This co-translational modification of the N terminus stabilizes diverse cytosolic plant proteins. The evolutionary conser
Externí odkaz:
https://doaj.org/article/ff204367416745e1aad4c13986b70397
Autor:
Leo Kiss, Tyler Rhinesmith, Jakub Luptak, Claire F. Dickson, Jonas Weidenhausen, Shannon Smyly, Ji-Chun Yang, Sarah L. Maslen, Irmgard Sinning, David Neuhaus, Dean Clift, Leo C. James
Publikováno v:
Nature Communications, Vol 14, Iss 1, Pp 1-17 (2023)
Abstract TRIM proteins are the largest family of E3 ligases in mammals. They include the intracellular antibody receptor TRIM21, which is responsible for mediating targeted protein degradation during Trim-Away. Despite their importance, the ubiquitin
Externí odkaz:
https://doaj.org/article/9847497c03534f53b81f80ff92484d91
Autor:
Komal Soni, Anusree Sivadas, Attila Horvath, Nikolay Dobrev, Rippei Hayashi, Leo Kiss, Bernd Simon, Klemens Wild, Irmgard Sinning, Tamás Fischer
Publikováno v:
Nature Communications, Vol 14, Iss 1, Pp 1-20 (2023)
Here the authors show how the MTREC core protein Red1 binds to and sequesters Pla1 from the 3’-end processing machinery to hyperadenylate cryptic unstable transcripts and target them to the exosome for efficient degradation.
Externí odkaz:
https://doaj.org/article/5f24d77b0a42478b8ce5d6cb4560dacd
Publikováno v:
Nature Communications, Vol 13, Iss 1, Pp 1-12 (2022)
High-resolution cryo-EM structures of a thermophilic 80S ribosome in two rotational states in complex with the protective factor Stm1, eEF2, and nascent chains are presented, providing insights into rRNA modifications and eukaryotic translation.
Externí odkaz:
https://doaj.org/article/9b5e27fbd2774bc293b6a2eed3cb89c0
Autor:
Nikolay Dobrev, Yasar Luqman Ahmed, Anusree Sivadas, Komal Soni, Tamás Fischer, Irmgard Sinning
Publikováno v:
Nature Communications, Vol 12, Iss 1, Pp 1-13 (2021)
The human PAXT complex and the MTREC complex in fission yeast are important exosome cofactors, serving in the degradation of specific noncoding RNAs. Here, the authors combine structural, biochemical and in vivo methods to show how Red1 recruits the
Externí odkaz:
https://doaj.org/article/a741735b27b946b7bd59c8534c1eb5c6
Autor:
Komal Soni, Georg Kempf, Karen Manalastas-Cantos, Astrid Hendricks, Dirk Flemming, Julien Guizetti, Bernd Simon, Friedrich Frischknecht, Dmitri I. Svergun, Klemens Wild, Irmgard Sinning
Publikováno v:
Communications Biology, Vol 4, Iss 1, Pp 1-14 (2021)
The SRP Alu domain is involved in co-translational protein targeting. Soni et al. investigate the Alu domain of Plasmodium falciparum, the agent of malaria, and find that unlike any other it adopts an open conformation.
Externí odkaz:
https://doaj.org/article/209bda6b89384eceb72f2290525335c3