Results 151 to 160 of about 1,391,894 (226)

Structural and biochemical analysis of a B12 superbinder

FEBS Letters, EarlyView.
BtuG proteins are vitamin B12 scavengers in Bacteroides thetaiotaomicron, a dominant human gut bacterium. We present crystal structures of three BtuG homologs bound to cobalamin and its precursor cobinamide, revealing picomolar binding affinities, among the highest known for any natural protein.
Jose M. Martinez Felices, Jacob J. Whittaker, Dirk J. Slotboom, Albert Guskov   +3 more
wiley   +1 more source

Genome-Wide DNA Methylation and Restriction-Modification Systems in <i>Casimicrobium huifangae</i> SJ-1, One of the Core Bacteria in Activated Sludge. [PDF]

Microorganisms
Yi J, Zhu K, Liu ZS, Si M, Sun H, Huang H, Jiang H, Liu SJ, Wang S.   +8 more
europepmc   +1 more source

Delineation of a lactococcal conjugation system reveals a restriction-modification evasion system. [PDF]

Microb Biotechnol, 2023
Ortiz Charneco G, Kelleher P, Buivydas A, Dashko S, de Waal PP, van Peij NNME, Roberts RJ, Mahony J, van Sinderen D.   +8 more
europepmc   +1 more source

Structures of mycobacterial 3‐methylcrotonyl‐CoA carboxylase reveal carrier‐domain translocation between catalytic sites

FEBS Letters, EarlyView.
Mycobacterial 3‐methylcrotonyl‐CoA carboxylase uses a mobile biotin‐carrying domain to shuttle a carboxyl group between two catalytic sites, enabling carboxylation of 3‐methylcrotonyl‐CoA during leucine breakdown. Cryo‐electron microscopy captures the carrier at both sites and reveals an inward loop movement that may prevent futile rebinding to the ...
Ajit Yadav, Bogdan I. Florea, Sebastian Geibel   +2 more
wiley   +1 more source

Biology of host-dependent restriction-modification in prokaryotes. [PDF]

EcoSal Plus
Anton BP, Blumenthal R, Eaglesham JB, Mruk I, Roberts RJ, Xu S-y, Weigele PR, Raleigh EA.   +7 more
europepmc   +1 more source

A sequential one-pot approach for rapid and convenient characterization of putative restriction-modification systems. [PDF]

mSystems, 2023
Zhang Y, Takaki Y, Yoshida-Takashima Y, Hiraoka S, Kurosawa K, Nunoura T, Takai K.   +6 more
europepmc   +1 more source

From junk to function — How weak selection in eukaryotes builds new parts and drives genomic complexity

FEBS Letters, EarlyView.
How do genomes gain new functional parts? In eukaryotes, which tend to evolve under weak selection, much of the genome is junk. Palazzo and Qiu borrow the logic of Markov chains to show how non‐functional DNA becomes functional through the appearance of intermediate states, which arise due to epistasis, buffering, and biochemical messiness, allowing ...
Alexander F. Palazzo, Yi Qiu
wiley   +1 more source

Acquisition of a novel restriction modification system regulates genetic flux and gene expression in the hypervirulent and globally disseminated CC17 lineage of group B Streptococcus. [PDF]

Nucleic Acids Res
Alves J, Crestani C, Marroquin SM, Johnston ABE, Ring N, Bowen C, Reglinski M, Doran KS, Zadoks RN, Lynskey NN.   +9 more
europepmc   +1 more source

Enhanced transformation efficiency in Treponema denticola enabled by SyngenicDNA-based plasmids lacking restriction-modification target motifs. [PDF]

Mol Oral Microbiol, 2023
Johnston CD, Goetting-Minesky MP, Kennedy K, Godovikova V, Zayed SM, Roberts RJ, Fenno JC.   +6 more
europepmc   +1 more source

The Shewanella oneidensis Fic enzyme SoFic targets the switch‐I region of EF‐Tu for AMPylation

FEBS Letters, EarlyView.
Fic enzymes mediate diverse post‐translational modifications across all domains of life, including AMPylation. Prokaryotic EF‐Tu can be AMPylated and deAMPylated by the conserved Fic enzyme SoFic. Structural and biochemical approaches were used to characterize the effect of AMPylation on EF‐Tu, SoFic's enzymatic activities, and the enzyme‐target ...
Svenja Runge, Vivian Pogenberg, Alexander Baumgart, Bente Siebels, Hartmut Schlüter, Michael Hecht‐Bucher, Aymelt Itzen   +6 more
wiley   +1 more source