scholarly journals Synthetic post‐translational modifications of elongation factor P using the ligase EpmA

FEBS Journal ◽  
2020 ◽  
Author(s):  
Miriam Pfab ◽  
Pavel Kielkowski ◽  
Ralph Krafczyk ◽  
Wolfram Volkwein ◽  
Stephan A. Sieber ◽  
...  
Keyword(s):  
Elongation Factor ◽  
Post Translational Modifications ◽  
Elongation Factor P

scholarly journals A Conserved Proline Triplet in Val-tRNA Synthetase and the Origin of Elongation Factor P

Cell Reports ◽  
2014 ◽  
Vol 9 (2) ◽  
pp. 476-483 ◽  
Author(s):  
Agata L. Starosta ◽  
Jürgen Lassak ◽  
Lauri Peil ◽  
Gemma C. Atkinson ◽  
Christopher J. Woolstenhulme ◽  
...  
Keyword(s):  
Elongation Factor ◽  
Trna Synthetase ◽  
Elongation Factor P

scholarly journals Posttranslational modification of Elongation Factor P from Staphylococcus aureus

FEBS Open Bio ◽  
2020 ◽  
Vol 10 (7) ◽  
pp. 1342-1347
Author(s):  
Alexander Golubev ◽  
Luc Negroni ◽  
Filipp Krasnovid ◽  
Shamil Validov ◽  
Gulnara Yusupova ◽  
...  
Keyword(s):  
Staphylococcus Aureus ◽  
Posttranslational Modification ◽  
Elongation Factor ◽  
Elongation Factor P

scholarly journals Loss of Elongation Factor P Disrupts Bacterial Outer Membrane Integrity

2012 ◽  
Vol 194 (16) ◽  
pp. 4484-4484 ◽  
Author(s):  
S. B. Zou ◽  
S. J. Hersch ◽  
H. Roy ◽  
J. B. Wiggers ◽  
A. S. Leung ◽  
...  
Keyword(s):  
Outer Membrane ◽  
Membrane Integrity ◽  
Elongation Factor ◽  
Bacterial Outer Membrane ◽  
Elongation Factor P

scholarly journals Crystal structure of elongation factor P from Thermus thermophilus HB8

2004 ◽  
Vol 101 (26) ◽  
pp. 9595-9600 ◽  
Author(s):  
K. Hanawa-Suetsugu ◽  
S.-i. Sekine ◽  
H. Sakai ◽  
C. Hori-Takemoto ◽  
T. Terada ◽  
...  
Keyword(s):  
Crystal Structure ◽  
Thermus Thermophilus ◽  
Elongation Factor ◽  
Thermus Thermophilus Hb8 ◽  
Elongation Factor P

scholarly journals Arginine-rhamnosylation as new strategy to activate translation elongation factor P

2015 ◽  
Vol 11 (4) ◽  
pp. 266-270 ◽  
Author(s):  
Jürgen Lassak ◽  
Eva C Keilhauer ◽  
Maximilian Fürst ◽  
Kristin Wuichet ◽  
Julia Gödeke ◽  
...  
Keyword(s):  
Elongation Factor ◽  
Translation Elongation Factor ◽  
Translation Elongation ◽  
New Strategy ◽  
Elongation Factor P

scholarly journals Elongation Factor P Interactions with the Ribosome Are Independent of Pausing

mBio ◽  
2017 ◽  
Vol 8 (4) ◽  
Author(s):  
Rodney Tollerson ◽  
Anne Witzky ◽  
Michael Ibba
Keyword(s):  
Single Molecule ◽  
Bond Formation ◽  
Elongation Factor ◽  
Peptide Bond ◽  
Cellular Distribution ◽  
Peptide Bond Formation ◽  
Translation Elongation ◽  
Single Molecule Tracking ◽  
Localization Pattern ◽  
Elongation Factor P

ABSTRACT Bacterial elongation factor P (EF-P) plays a pivotal role in the translation of polyproline motifs. To stimulate peptide bond formation, EF-P must enter the ribosome via an empty E-site. Using fluorescence-based single-molecule tracking, Mohapatra et al. (S. Mohapatra, H. Choi, X. Ge, S. Sanyal, and J. C. Weisshaar, mBio 8:e00300-17, 2017, https://doi.org/10.1128/mBio.00300-17 !) monitored the cellular distribution of EF-P and quantified the frequency of association between EF-P and the ribosome under various conditions. Findings from the study showed that EF-P has a localization pattern that is strikingly similar to that of ribosomes. Intriguingly, EF-P was seen to bind ribosomes more frequently than the estimated number of pausing events, indicating that E-site vacancies occur even when ribosomes are not paused. The study provides new insights into the mechanism of EF-P-dependent peptide bond formation and the intricacies of translation elongation.

scholarly journals (R)-β-Lysine-modified Elongation Factor P Functions in Translation Elongation

2012 ◽  
Vol 288 (6) ◽  
pp. 4416-4423 ◽  
Author(s):  
Tammy J. Bullwinkle ◽  
S. Betty Zou ◽  
Andrei Rajkovic ◽  
Steven J. Hersch ◽  
Sara Elgamal ◽  
...  
Keyword(s):  
Elongation Factor ◽  
Translation Elongation ◽  
Elongation Factor P
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