RT Journal Article
SR Electronic
T1 Toward D-peptide biosynthesis: Elongation Factor P enables ribosomal incorporation of consecutive D-amino acids
JF bioRxiv
FD Cold Spring Harbor Laboratory
SP 125930
DO 10.1101/125930
A1 Po-Yi Huang
A1 Fanny Wang
A1 Kamesh Narasimhan
A1 Kelly Chatman
A1 John Aach
A1 Sunia A. Trauger
A1 Ryan Spoering
A1 George M. Church
YR 2017
UL http://biorxiv.org/content/early/2017/04/10/125930.abstract
AB To maintain stereospecific biochemistry in cells, living organisms have evolved mechanisms to exclude D-amino acids (DAA) in their protein synthesis machinery, which also limits our exploration of the realm of mirror-image molecules. Here, we show that high affinity between EF-Tu and aminoacyl-tRNA promotes D-amino acid incorporation. More strikingly, Elongation Factor P efficiently resolves peptidyl transferase stalling between two consecutive D-amino acids, and hence enables the translation of D-peptides.