Zobrazeno 1 - 10
of 209
pro vyhledávání: '"Tania A Baker"'
Publikováno v:
eLife, Vol 9 (2020)
AAA+ proteases perform regulated protein degradation in all kingdoms of life and consist of a hexameric AAA+ unfoldase/translocase in complex with a self-compartmentalized peptidase. Based on asymmetric features of cryo-EM structures and a sequential
Externí odkaz:
https://doaj.org/article/a60053f5c3f7400988af78e101b7ab9c
Publikováno v:
eLife, Vol 9 (2020)
When ribosomes fail to complete normal translation, all cells have mechanisms to ensure degradation of the resulting partial proteins to safeguard proteome integrity. In Escherichia coli and other eubacteria, the tmRNA system rescues stalled ribosome
Externí odkaz:
https://doaj.org/article/623a65ede5f24ec0a7f8e65a342d62ab
Autor:
Xue Fei, Tristan A Bell, Simon Jenni, Benjamin M Stinson, Tania A Baker, Stephen C Harrison, Robert T Sauer
Publikováno v:
eLife, Vol 9 (2020)
ClpXP is an ATP-dependent protease in which the ClpX AAA+ motor binds, unfolds, and translocates specific protein substrates into the degradation chamber of ClpP. We present cryo-EM studies of the E. coli enzyme that show how asymmetric hexameric rin
Externí odkaz:
https://doaj.org/article/4a7bb2bb3e33420786905516001192e8
Publikováno v:
eLife, Vol 9 (2020)
Mitochondria control the activity, quality, and lifetime of their proteins with an autonomous system of chaperones, but the signals that direct substrate-chaperone interactions and outcomes are poorly understood. We previously discovered that the mit
Externí odkaz:
https://doaj.org/article/63ad399fffd242d2b4db620d4cceb0bc
Publikováno v:
eLife, Vol 8 (2019)
Most AAA+ remodeling motors denature proteins by pulling on the peptide termini of folded substrates, but it is not well-understood how motors produce grip when resisting a folded domain. Here, at single amino-acid resolution, we identify the determi
Externí odkaz:
https://doaj.org/article/e7faaf7002144c348b88d43881ef349d
Autor:
Natalie Al-Furoukh, Julia R Kardon, Marcus Krüger, Marten Szibor, Tania A Baker, Thomas Braun
Publikováno v:
PLoS ONE, Vol 9, Iss 7, p e103141 (2014)
The mitochondrial matrix GTPase NOA1 is a nuclear encoded protein, essential for mitochondrial protein synthesis, oxidative phosphorylation and ATP production. Here, we demonstrate that newly translated NOA1 protein is imported into the nucleus, wher
Externí odkaz:
https://doaj.org/article/d258f328a49c4ca88a89785391b3e84b
Autor:
Alireza Ghanbarpour, Steven E. Cohen, Xue Fei, Laurel F. Kinman, Tristan A. Bell, Jia Jia Zhang, Tania A. Baker, Joseph H. Davis, Robert T. Sauer
Publikováno v:
Nature Communications, Vol 14, Iss 1, Pp 1-10 (2023)
Abstract AAA+ proteases degrade intracellular proteins in a highly specific manner. E. coli ClpXP, for example, relies on a C-terminal ssrA tag or other terminal degron sequences to recognize proteins, which are then unfolded by ClpX and subsequently
Externí odkaz:
https://doaj.org/article/f72b46a348b247609e8481dbe950089a
Autor:
Meghann R. Kasal, Hema Chandra Kotamarthi, Madeline M. Johnson, Hannah M. Stephens, Matthew J. Lang, Robert T. Sauer, Tania A. Baker
Publikováno v:
Cell Reports, Vol 42, Iss 9, Pp 113061- (2023)
Summary: Lon is a widely distributed AAA+ (ATPases associated with diverse cellular activities) protease known for degrading poorly folded and damaged proteins and is often classified as a weak protein unfoldase. Here, using a Lon-degron pair from Me
Externí odkaz:
https://doaj.org/article/9c5226e5cf5f463fae8dd0f9aa92d7bc
Publikováno v:
Nature Structural & Molecular Biology. 29:1068-1079
ClpAP, a two-ring AAA+ protease, degrades N-end-rule proteins bound by the ClpS adaptor. Here we present high-resolution cryo-EM structures of Escherichia coli ClpAPS complexes, showing how ClpA pore loops interact with the ClpS N-terminal extension
Publikováno v:
Molecular microbiologyREFERENCES.
Targeted protein degradation plays important roles in stress responses in all cells. In E. coli, the membrane-bound AAA+ FtsH protease degrades cytoplasmic and membrane proteins. Here, we demonstrate that FtsH degrades cyclopropane fatty acid (CFA) s