ArticleProtein science : a publication of the Protein Society2015
Hypothetical protein CT398 (CdsZ) interacts with σ(54) (RpoN)-holoenzyme and the type III secretion export apparatus in Chlamydia trachomatis.
Article in Protein science : a publication of the Protein Society, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 14 papers.
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Who cites it
14 citing papers in PubMed, 16 citations in OpenAlex.
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- Type III Secretion inMicrobiology and molecular biology reviews : MMBR · 2023Review
- Comparative Genomic Analysis of the DUF34 Protein Family Suggests Role as a Metal Ion Chaperone or Insertase.Biomolecules · 2021Article
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- Chlamydia muridarum Induces Pathology in the Female Upper Genital Tract via Distinct Mechanisms.Infection and immunity · 2019Article
- Identification of new DNA-associated proteins from Waddlia chondrophila.Scientific reports · 2019Article
- Chlamydia Spreading from the Genital Tract to the Gastrointestinal Tract - A Two-Hit Hypothesis.Trends in microbiology · 2018Review
- Crystal structure of the MSMEG_4306 gene product from Mycobacterium smegmatis.Acta crystallographica. Section F, Structural biology communications · 2018Article
- The Loss of Expression of a Single Type 3 Effector (CT622) Strongly ReducesFrontiers in cellular and infection microbiology · 2018Article
- Regulation ofEcoSal Plus · 2017Review
- Article
- Chlamydia cell biology and pathogenesis.Nature reviews. Microbiology · 2016Review
- A working model for the type III secretion mechanism in Chlamydia.Microbes and infection · 2016Review
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Authors and funding
4 authors at 2 institutions in 1 country.
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Abstract
A significant challenge to bacteriology is the relatively large proportion of proteins that lack sufficient sequence similarity to support functional annotation (i.e. hypothetical proteins). The aim of this study was to apply protein structural homology to gain insights into a candidate protein of unknown function (CT398) within the medically important, obligate intracellular bacterium Chlamydia trachomatis. C. trachomatis is a major human pathogen responsible for numerous infections throughout the world that can lead to blindness and infertility. A 2.12 Å crystal structure of hypothetical protein CT398 was determined that was comprised of N-terminal coiled-coil and C-terminal Zn-ribbon domains. The structure of CT398 displayed a high degree of structural similarity to FlgZ (Flagellar-associated zinc-ribbon domain protein) from Helicobacter pylori. This observation directed analyses of candidate protein partners of CT398, revealing interactions with two paralogous type III secretion system (T3SS) ATPase-regulators (CdsL and FliH) and the alternative sigma factor RpoN (σ(54) ). Furthermore, genetic introduction of a conditional expression, affinity-tagged construct into C. trachomatis enabled the purification of a CT398-RpoN-holoenzyme complex, suggesting a potential role for CT398 in modulating transcriptional activity during infection. The interactions reported here, in tandem with previous FlgZ studies in H. pylori, indicate that CT398 functions as a regulator of several key areas of chlamydial biology throughout the developmental cycle. Accordingly, we propose that CT398 be named CdsZ (Contact-dependent secretion-associated zinc-ribbon domain protein).
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