Structure of the Cytoplasmic Domain of the Flagellar Secretion Apparatus Component FlhA from Helicobacter pylori

Moore, Stanley A.; Jia, Yunhua

doi:10.1074/jbc.m110.119412

Cited by 41 publications

(26 citation statements)

References 52 publications

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“…2C). Analysis of truncated versions of YscV C revealed that the presence of all structural domains (SD) of YscV C (Bange et al ., 2010; Lilic et al ., 2010; Moore and Jia, 2010; Worrall et al ., 2010) was required for significant co‐purification of YscX and YscY (Fig. 2C and D, Fig.…”

Section: Resultsmentioning

confidence: 99%

Assembly of the Yersinia injectisome: the missing pieces

Diepold

Wiesand

Amstutz

et al. 2012

Molecular Microbiology

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Summary The assembly of the type III secretion injectisome culminates in the formation of the needle. In Yersinia, this step requires not only the needle subunit (YscF), but also the small components YscI, YscO, YscX and YscY. We found that these elements act after the completion of the transmembrane export apparatus. YscX and YscY co‐purified with the export apparatus protein YscV, even in the absence of any other protein. YscY‐EGFP formed fluorescent spots, suggesting its presence in multiple copies. YscO and YscX were required for export of the early substrates YscF, YscI and YscP, but were only exported themselves after the substrate specificity switch had occurred. Unlike its flagellar homologue FliJ, YscO was not required for the assembly of the ATPase YscN. Finally, we investigated the role of the small proteins in export across the inner membrane. No export of the reporter substrate YscP1–137‐PhoA into the periplasm was observed in absence of YscI, YscO or YscX, confirming that these proteins are required for export of the first substrates. In contrast, YscP1–137‐PhoA accumulated in the periplasm in the absence of YscF, suggesting that YscF is not required for the function of the export apparatus, but that its polymerization opens the secretin YscC.

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Section: Resultsmentioning

confidence: 99%

Assembly of the Yersinia injectisome: the missing pieces

Diepold

Wiesand

Amstutz

et al. 2012

Molecular Microbiology

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“…YscV has been shown to consist of an N‐terminal transmembrane part (amino acids 1–331) containing eight TM helices, and a C‐terminal cytosolic part (amino acids 332–704) (Plano et al ., 1991). The structure of the cytosolic domain of various homologues of YscV (Bange et al ., 2010; Lilic et al ., 2010; Moore and Jia, 2010; Worrall et al ., 2010) was shown to consist of four subdomains. The structural domain (SD) 2, corresponding to amino acids 442 to 494 of YscV, contains a ‘ring‐building motif’ (Lilic et al ., 2010; Worrall et al ., 2010) that had been previously found in all other ring‐forming components of the injectisome (Spreter et al ., 2009).…”

Section: Resultsmentioning

confidence: 99%

“…YscV, which was originally called LcrD, is highly conserved between different injectisomes and the flagellum (where it is called FlhA), and consists of an N‐terminal transmembrane (TM) domain (amino acids 1–331) including eight TM helices (Plano et al ., 1991), and a C‐terminal cytosolic part (amino acids 332–704). The cytosolic domain of various homologues of YscV was shown to consist of four structural domains (Bange et al ., 2010; Lilic et al ., 2010; Moore and Jia, 2010; Worrall et al ., 2010).…”

Section: Introductionmentioning

confidence: 99%

The assembly of the export apparatus (YscR,S,T,U,V) of the Yersinia type III secretion apparatus occurs independently of other structural components and involves the formation of an YscV oligomer

Diepold

Wiesand

Cornelis

2011

Molecular Microbiology

121

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“…FlhA L (residues 328 to 362) is unfolded in the crystal structure of the Salmonella FlhA C ; its N-terminal 19 residues (residues 328 to 346) are invisible, and the remaining 15 residues (residues 347 to 362) are in an extended conformation stabilized by the interaction with a neighboring molecule in the crystal packing (42). FlhA L in the FlhA C crystals of Helicobacter pylori (44) and Bacillus subtilis (16), however, adopts an ␣-helical structure. Therefore, it is possible that the FlhA L of the Salmonella FlhA C is folded into an ␣-helix when it interacts with FliJ.…”

Section: Discussionmentioning

confidence: 99%