The distinct anchoring mechanism of FtsY from different microbes.
The SRP receptor FtsY, which is involved in targeting and translocating membrane protein, is generally composed of the N-terminal domain and the NG domain. Although FtsY was highly homologous in the composition of amino acids and functions among microbes, the different mechanism in the location of FtsYs from different bacteria such as S. coelicolor and E. coli were discovered in this study by laser scanning confocal microscope (LSCM) in vivo and molecular techniques in vitro. The results revealed that the N-terminal domain of S. coelicolor FtsY was indispensable for FtsY's anchoring membrane, and while the A domain of E. coli FtsY was dispensable. Moreover, the A domain of E. coli FtsY might promote itself to bind the membrane depending on the location images and Western blotting.
Dong
Hui-Jun
HJ
R&D Center, Lunan Pharmaceutical Company, Linyi, 276005, China. dhjjjy@gmail.com
Jiang
Jun-Yun
JY
Li
Yong-Quan
YQ
D001426:Bacterial Proteins / Q000235:genetics / Q000378:metabolism*; D004926:Escherichia coli / Q000378:metabolism*; D008565:Membrane Proteins / Q000378:metabolism*; D008958:Models, Molecular; D017434:Protein Structure, Tertiary; D021381:Protein Transport; D018160:Receptors, Cytoplasmic and Nuclear / Q000235:genetics / Q000378:metabolism*; D048372:Streptomyces coelicolor / Q000378:metabolism*
D001426:Bacterial Proteins; C087406:FtsY protein, Bacteria; D008565:Membrane Proteins; D018160:Receptors, Cytoplasmic and Nuclear