The twin-arginine transport (Tat) system is essential for cell viability in Sinorhizobium meliloti and may play a role during the development of root nodules. Utilizing an in vivo recombination strategy, we have constructed 28 strains that contain deletions in predicted Tat substrates. Testing of these mutations for symbiotic proficiency on the plant hosts alfalfa and sweet clover shows that some of these mutations affect associations with these hosts differentially.
Download full-text PDF |
Source |
---|---|
http://www.ncbi.nlm.nih.gov/pmc/articles/PMC3457499 | PMC |
http://dx.doi.org/10.1128/AEM.01458-12 | DOI Listing |
Unlabelled: The chloroplast Twin Arginine Transport (cpTAT) protein translocation pathway is one of the thylakoid membrane's two protein transport pathways for getting proteins into the lumen. The cpTAT system distinguishes itself by transporting fully folded proteins across the thylakoid, using the sole energy source of the proton motive force (PMF). The cpTAT pathway is evolutionarily conserved with the TAT pathway found in many bacteria and archaea.
View Article and Find Full Text PDFWorld J Microbiol Biotechnol
July 2024
University School of Biotechnology, Guru Gobind Singh Indraprastha University, Sec 16C Dwarka, New Delhi, 110078, India.
Pseudomonas aeruginosa PR23 isolated from the hydrocarbon contaminated soil can tolerate and degrade mixture of polyaromatic hydrocarbons (PAHs) at an initial concentration of 1300 ppm. The degradation and intermediates formed were assessed by gas chromatography-mass spectrometry (GC-MS) analysis. The isolated strain was able to degrade 59.
View Article and Find Full Text PDFAppl Environ Microbiol
July 2024
Hubei Key Laboratory of Cell Homeostasis, College of Life Sciences, Wuhan University, Wuhan, China.
Unlabelled: To cope with a high-salinity environment, haloarchaea generally employ the twin-arginine translocation (Tat) pathway to transport secretory proteins across the cytoplasm membrane in a folded state, including Tat-dependent extracellular subtilases (halolysins) capable of autocatalytic activation. Some halolysins, such as SptA of J7-2, are produced at late-log phase to prevent premature enzyme activation and proteolytic damage of cellular proteins in haloarchaea; however, the regulation mechanism for growth phase-dependent expression of halolysins remains largely unknown. In this study, a DNA-protein pull-down assay was performed to identify the proteins binding to the 5'-flanking sequence of encoding halolysin SptA in strain J7-2, revealing a TrmBL2-like transcription factor (NgTrmBL2).
View Article and Find Full Text PDFPLoS One
June 2024
Institute of Microbiology, Leibniz Universität Hannover, Hanover, Germany.
SlyD is a widely-occurring prokaryotic FKBP-family prolyl isomerase with an additional chaperone domain. Often, such as in Escherichia coli, a third domain is found at its C-terminus that binds nickel and provides it for nickel-enzyme biogenesis. SlyD has been found to bind signal peptides of proteins that are translocated by the Tat pathway, a system for the transport of folded proteins across membranes.
View Article and Find Full Text PDFSci Rep
June 2024
Institute of Microbiology, Leibniz Universität Hannover, Herrenhäuser Straße 2, 30419, Hannover, Germany.
The twin-arginine translocation (Tat) system transports folded proteins across energized biological membranes in bacteria, plastids, and plant mitochondria. In Escherichia coli, the three membrane proteins TatA, TatB and TatC associate to enable Tat transport. While TatB and TatC together form complexes that bind Tat-dependently transported proteins, the TatA component is responsible for the permeabilization of the membrane during transport.
View Article and Find Full Text PDFEnter search terms and have AI summaries delivered each week - change queries or unsubscribe any time!