Zobrazeno 1 - 10
of 80
pro vyhledávání: '"Günter Kramer"'
Autor:
Melania Minoia, Jany Quintana-Cordero, Katharina Jetzinger, Ilgin Eser Kotan, Kathryn Jane Turnbull, Michela Ciccarelli, Anna E. Masser, Dorina Liebers, Eloïse Gouarin, Marius Czech, Vasili Hauryliuk, Bernd Bukau, Günter Kramer, Claes Andréasson
Publikováno v:
Nature Communications, Vol 15, Iss 1, Pp 1-16 (2024)
Abstract Cotranslational protein folding depends on general chaperones that engage highly diverse nascent chains at the ribosomes. Here we discover a dedicated ribosome-associated chaperone, Chp1, that rewires the cotranslational folding machinery to
Externí odkaz:
https://doaj.org/article/f23814c7fcb4463299135165d37e841c
Autor:
Jonathan Bohlen, Liza Harbrecht, Saioa Blanco, Katharina Clemm von Hohenberg, Kai Fenzl, Günter Kramer, Bernd Bukau, Aurelio A. Teleman
Publikováno v:
Nature Communications, Vol 11, Iss 1, Pp 1-15 (2020)
Upon stress, translation of ATF4 is induced by reinitiating ribosomes following translation of short upstream open reading frames (uORFs). Here the authors show that translation re-initiation of ATF4 is mediated by the DENR-MCTS1 complex which acts o
Externí odkaz:
https://doaj.org/article/6f5c73c82bd545db83b3c936664b634c
Autor:
Lisa Teubner, Renate Frantz, Luigi La Pietra, Martina Hudel, Jasmin Bazant, Günter Lochnit, Lena Eismann, Günter Kramer, Trinad Chakraborty, Mobarak Abu Mraheil
Publikováno v:
International Journal of Molecular Sciences, Vol 23, Iss 23, p 15021 (2022)
Protein secretion plays a central role in modulating interactions of the human pathogen Listeria monocytogenes with its environment. Recently, secretion of RNA has emerged as an important strategy used by the pathogen to manipulate the host cell resp
Externí odkaz:
https://doaj.org/article/efd68f56e1584a4b82912730c2d28e9b
Publikováno v:
Frontiers in Molecular Biosciences, Vol 8 (2021)
Growing cells invest a significant part of their biosynthetic capacity into the production of proteins. To become functional, newly-synthesized proteins must be N-terminally processed, folded and often translocated to other cellular compartments. A g
Externí odkaz:
https://doaj.org/article/349eaa4bd69f478fa3ccf7e93ece82b1
Autor:
Mohammed Jamshad, Timothy J Knowles, Scott A White, Douglas G Ward, Fiyaz Mohammed, Kazi Fahmida Rahman, Max Wynne, Gareth W Hughes, Günter Kramer, Bernd Bukau, Damon Huber
Publikováno v:
eLife, Vol 8 (2019)
In bacteria, the translocation of proteins across the cytoplasmic membrane by the Sec machinery requires the ATPase SecA. SecA binds ribosomes and recognises nascent substrate proteins, but the molecular mechanism of nascent substrate recognition is
Externí odkaz:
https://doaj.org/article/03c1fc4e168e4c638fbfaa1f143e7620
Autor:
Ajeet K Sharma, Pietro Sormanni, Nabeel Ahmed, Prajwal Ciryam, Ulrike A Friedrich, Günter Kramer, Edward P O'Brien
Publikováno v:
PLoS Computational Biology, Vol 15, Iss 5, p e1007070 (2019)
Analysis methods based on simulations and optimization have been previously developed to estimate relative translation rates from next-generation sequencing data. Translation involves molecules and chemical reactions, hence bioinformatics methods con
Externí odkaz:
https://doaj.org/article/0de2347b544d46a793ed36407ad3ef9f
Autor:
Daniel A. Nissley, Ajeet K. Sharma, Nabeel Ahmed, Ulrike A. Friedrich, Günter Kramer, Bernd Bukau, Edward P. O’Brien
Publikováno v:
Nature Communications, Vol 7, Iss 1, Pp 1-13 (2016)
The folding of protein domains can occur concomitant with their synthesis, and the rates at which individual codons are translated by the ribosome can affect the folding process. Here the authors present a kinetic model that accurately predicts the p
Externí odkaz:
https://doaj.org/article/644393080ecd46ffb8ae9c3eca310651
Autor:
Lucia Grenga, Govind Chandra, Gerhard Saalbach, Carla V. Galmozzi, Günter Kramer, Jacob G. Malone
Publikováno v:
Frontiers in Microbiology, Vol 8 (2017)
The ability of bacteria to respond to environmental change is based on the ability to coordinate, redirect and fine-tune their genetic repertoire as and when required. While we can learn a great deal from reductive analysis of individual pathways and
Externí odkaz:
https://doaj.org/article/5d57d1ce1038446db156b4fa6e15cfff
Publikováno v:
PLoS ONE, Vol 9, Iss 6, p e99395 (2014)
Incorporating fluorescent amino acids by suppression of the TAG amber codon is a useful tool for site-specific labeling of proteins and visualizing their localization in living cells. Here we use a plasmid encoded orthogonal tRNA/aminoacyl-tRNA synth
Externí odkaz:
https://doaj.org/article/b7fb307737de46b2a3619a2ef25169e7
Autor:
Maximilian O Press, Hui Li, Nicole Creanza, Günter Kramer, Christine Queitsch, Victor Sourjik, Elhanan Borenstein
Publikováno v:
PLoS Genetics, Vol 9, Iss 7, p e1003631 (2013)
The molecular chaperone Hsp90 is essential in eukaryotes, in which it facilitates the folding of developmental regulators and signal transduction proteins known as Hsp90 clients. In contrast, Hsp90 is not essential in bacteria, and a broad characteri
Externí odkaz:
https://doaj.org/article/ee430ee86ce74ec7813da0754723168f