scholarly journals Release Factor Inhibiting Antimicrobial Peptides Improve Nonstandard Amino Acid Incorporation in Wild-type Bacterial Cells

2020 ◽  
Vol 15 (7) ◽  
pp. 1852-1861 ◽  
Author(s):  
Erkin Kuru ◽  
Rosa-Maria Määttälä ◽  
Karen Noguera ◽  
Devon A. Stork ◽  
Kamesh Narasimhan ◽  
...  
2005 ◽  
Vol 51 (8) ◽  
pp. 715-718 ◽  
Author(s):  
Phyllis C Braun

Farnesol, a quorum sensing (QS) signal, is produced by Candida albicans during high density growth and has been found to inhibit morphogenesis. This QS auto-inducing signal was discovered to increase amino acid incorporation by C. albicans when concentrations of farnesol increased to 10 µg/mL in yeast nitrogen broth. Farnesol concentrations greater than 10 µg/mL abolished the enhanced incorporation, and the magnitude of the increased incorporation was dependent on cell-surface hydrophobicity.Key words: Candida albicans, farnesol, amino acid incorporation.


2016 ◽  
Vol 12 (6) ◽  
pp. 1746-1749 ◽  
Author(s):  
Yunan Zheng ◽  
Marc J. Lajoie ◽  
James S. Italia ◽  
Melissa A. Chin ◽  
George M. Church ◽  
...  

Unconditional deletion of RF1 in a genomically recoded E. coli enables multisite noncanonical amino acid incorporation by UAG suppression.


Amino Acids ◽  
2020 ◽  
Author(s):  
Thomas L. Williams ◽  
Debra J. Iskandar ◽  
Alexander R. Nödling ◽  
Yurong Tan ◽  
Louis Y. P. Luk ◽  
...  

AbstractGenetic code expansion is a powerful technique for site-specific incorporation of an unnatural amino acid into a protein of interest. This technique relies on an orthogonal aminoacyl-tRNA synthetase/tRNA pair and has enabled incorporation of over 100 different unnatural amino acids into ribosomally synthesized proteins in cells. Pyrrolysyl-tRNA synthetase (PylRS) and its cognate tRNA from Methanosarcina species are arguably the most widely used orthogonal pair. Here, we investigated whether beneficial effect in unnatural amino acid incorporation caused by N-terminal mutations in PylRS of one species is transferable to PylRS of another species. It was shown that conserved mutations on the N-terminal domain of MmPylRS improved the unnatural amino acid incorporation efficiency up to five folds. As MbPylRS shares high sequence identity to MmPylRS, and the two homologs are often used interchangeably, we examined incorporation of five unnatural amino acids by four MbPylRS variants at two temperatures. Our results indicate that the beneficial N-terminal mutations in MmPylRS did not improve unnatural amino acid incorporation efficiency by MbPylRS. Knowledge from this work contributes to our understanding of PylRS homologs which are needed to improve the technique of genetic code expansion in the future.


1955 ◽  
Vol 215 (1) ◽  
pp. 111-124 ◽  
Author(s):  
Henry Borsook ◽  
Adolph Abrams ◽  
Peter H. Lowy

1954 ◽  
Vol 210 (2) ◽  
pp. 837-849 ◽  
Author(s):  
M. Rabinovitz ◽  
Margaret E. Olson ◽  
David M. Greenberg

Sign in / Sign up

Export Citation Format

Share Document