title: Molecular characterization of the InvE regulator in the secretion of type III secretion translocases in Salmonella enterica serovar Typhimurium.
abstract: The type III secretion systems (T3SSs) are exploited by many Gram-negative pathogenic bacteria to deliver a set of effector proteins into the host cytosol during cell entry. The T3SS of Salmonella enterica serovar Typhimurium is composed of more than 20 proteins that constitute the membrane-associated base, the needle and the tip complex at the distal end of the T3SS needle. Membrane docking and piercing between the T3SS and host cells is followed by the secretion of effector proteins. Therefore, a secretion hierarchy among the substrates of the T3SS is required. The secretion of the pore-forming translocase proteins SipB, SipC and SipD is controlled by the T3SS regulator protein, InvE. During an attempt to identify the regions of InvE that are involved in T3SS regulation, it was observed that the secretion of SipB, SipC and SipD was inhibited when the C-terminal 52 amino acids were removed from InvE. In addition, InvE derivatives lacking the N-terminal 30 and 100 residues were unable to secrete translocases into the culture medium. Interestingly, in the absence of the N-terminal 180 residues of InvE, SipD is unstable, resulting in the hypersecretion of SipB. We also found that both the type III secretion signals of SipB and SptP were functionally interchangeable with the first 30 amino acids of InvE, which could allow the secretion of a reporter protein. These results indicate that InvE may have two functional domains responsible for regulating the secretion of translocases: an N-terminal secretion signal and a C-terminal regulatory domain.
authors.affiliation: School of Life Sciences and Biotechnology, Korea University, Seoul 136-701, Republic of Korea.
authors.forename: Jin Seok
authors.initials: JS
authors.lastname: Kim
authors.affiliation: School of Life Sciences and Biotechnology, Korea University, Seoul 136-701, Republic of Korea.
authors.forename: Jung Im
authors.initials: JI
authors.lastname: Jang
authors.affiliation: School of Life Sciences and Biotechnology, Korea University, Seoul 136-701, Republic of Korea.
authors.forename: Jeong Seon
authors.initials: JS
authors.lastname: Eom
authors.affiliation: School of Life Sciences and Biotechnology, Korea University, Seoul 136-701, Republic of Korea.
authors.forename: Chang Heon
authors.initials: CH
authors.lastname: Oh
authors.affiliation: School of Life Sciences and Biotechnology, Korea University, Seoul 136-701, Republic of Korea.
authors.forename: Hyeon Guk
authors.initials: HG
authors.lastname: Kim
authors.affiliation: School of Life Sciences and Biotechnology, Korea University, Seoul 136-701, Republic of Korea.
authors.forename: Bae Hoon
authors.initials: BH
authors.lastname: Kim
authors.affiliation: Department of Microbiology and Immunology, Chosun University School of Dentistry, Gwang ju 501-759, Republic of Korea.
authors.forename: Iel Soo
authors.initials: IS
authors.lastname: Bang
authors.affiliation: Department of Biological Science, Hanseo University, Chungcheongnam-do 356-706, Republic of Korea.
authors.forename: Seong Ho
authors.initials: SH
authors.lastname: Bang
authors.affiliation: School of Life Sciences and Biotechnology, Korea University, Seoul 136-701, Republic of Korea.
authors.forename: Yong Keun
authors.initials: YK
authors.lastname: Park
mesh_terms: D001426:Bacterial Proteins / Q000378:metabolism*; D058947:Bacterial Secretion Systems; D004252:DNA Mutational Analysis; D010458:Peptidyl Transferases / Q000378:metabolism*; D017434:Protein Structure, Tertiary; D012486:Salmonella typhimurium / Q000235:genetics* / Q000378:metabolism*
chemical_list: D001426:Bacterial Proteins; D058947:Bacterial Secretion Systems; D010458:Peptidyl Transferases