Hayashi Fumio, Kawashima Yurie, Takeuchi Shinobu, Okimori Kensuke, Inobe Eri, Oosawa Kenji
a Division of Molecular Science, Faculty of Science and Technology , Gunma University , Kiryu , Japan.
Biosci Biotechnol Biochem. 2014;78(9):1560-3. doi: 10.1080/09168451.2014.921552. Epub 2014 Jun 12.
SptP is a virulence effector protein of Salmonella that is involved in bacterial invasion into a host cell. For effective secretion, SptP forms a complex with SptP-specific chaperone SicP through its chaperone-binding domain, residues 35-139. Here, we suggest the possibility that residues 106-136 of SptP are important for complex formation with SicP by in vitro reconstitution experiments.
SptP是沙门氏菌的一种毒力效应蛋白,参与细菌对宿主细胞的侵袭。为了实现有效分泌,SptP通过其伴侣结合结构域(第35至139位氨基酸残基)与SptP特异性伴侣蛋白SicP形成复合物。在此,我们通过体外重组实验表明,SptP的第106至136位氨基酸残基对于与SicP形成复合物可能很重要。