Over the past decade the number and variety of protein post-translational modifications that
have been detected and characterized in bacteria have rapidly increased. Most post …

This review summarizes our current understanding of translation in prokaryotes, focusing on
the mechanistic and structural aspects of each phase of translation: initiation, elongation …

Lactylation was initially discovered on human histones. Given its nascence, its occurrence
on nonhistone proteins and downstream functional consequences remain elusive. Here we …

Within the canonical repertoire of the amino acid involved in protein biogenesis, proline
plays a unique role as an amino acid presenting a modified backbone rather than a side …

Although nanopores can be used for single-molecule sequencing of nucleic acids using low-
cost portable devices, the characterization of proteins and their modifications has yet to be …

Ribosomes translate genetic information into polypeptides in several basic steps: initiation,
elongation, termination and recycling. When ribosomes are arrested during elongation or …

Ribosomes synthesizing proteins containing consecutive proline residues become stalled
and require rescue via the action of uniquely modified translation elongation factors, EF-P in …

The prokaryotic translation elongation factor P (EF-P) and the eukaryotic/archaeal
counterparts eIF5A/aIF5A are proteins that serve a crucial role in mitigating ribosomal …

Efficiency of protein synthesis on the ribosome is strongly affected by the amino acid
composition of the assembled amino acid chain. Challenging sequences include proline …

During protein synthesis, ribosomes become stalled on polyproline-containing sequences,
unless they are rescued in archaea and eukaryotes by the initiation factor 5A (a/eIF-5A) and …