ArticleJournal of bacteriology1991
Localization of the Mycoplasma pneumoniae cytadherence-accessory proteins HMW1 and HMW4 in the cytoskeletonlike Triton shell.
Article in Journal of bacteriology, 1991. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 35 papers.
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
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Who cites it
35 citing papers in PubMed, 79 citations in OpenAlex.
- Imaging Minimal Bacteria at the Nanoscale: a Reliable and Versatile Process to Perform Single-Molecule Localization Microscopy in Mycoplasmas.Microbiology spectrum · 2022Article
- Electron cryotomography of Mycoplasma pneumoniae mutants correlates terminal organelle architectural features and function.Molecular microbiology · 2018Article
- P65 truncation impacts P30 dynamics during Mycoplasma pneumoniae gliding.Journal of bacteriology · 2012Article
- Insights into the function of Mycoplasma pneumoniae protein P30 from orthologous gene replacement.Microbiology (Reading, England) · 2011Article
- Domain analysis of protein P30 in Mycoplasma pneumoniae cytadherence and gliding motility.Journal of bacteriology · 2011Article
- Functional domain analysis of the Mycoplasma pneumoniae co-chaperone TopJ.Molecular microbiology · 2010Article
- Mycoplasma pneumoniae cytoskeletal protein HMW2 and the architecture of the terminal organelle.Journal of bacteriology · 2009Article
- Mycoplasma pneumoniae J-domain protein required for terminal organelle function.Molecular microbiology · 2009Article
- Functional analysis of the Mycoplasma genitalium MG312 protein reveals a specific requirement of the MG312 N-terminal domain for gliding motility.Journal of bacteriology · 2007Article
- Transposon mutagenesis identifies genes associated with Mycoplasma pneumoniae gliding motility.Journal of bacteriology · 2006Article
- Mutant analysis reveals a specific requirement for protein P30 in Mycoplasma pneumoniae gliding motility.Journal of bacteriology · 2005Article
- HMW1 is required for stability and localization of HMW2 to the attachment organelle of Mycoplasma pneumoniae.Journal of bacteriology · 2004Article
- Use of fluorescent-protein tagging to determine the subcellular localization of mycoplasma pneumoniae proteins encoded by the cytadherence regulatory locus.Journal of bacteriology · 2004Article
- Attachment organelle formation represented by localization of cytadherence proteins and formation of the electron-dense core in wild-type and mutant strains of Mycoplasma pneumoniae.Journal of bacteriology · 2003Article
- Characterization of a Mycoplasma pneumoniae hmw3 mutant: implications for attachment organelle assembly.Journal of bacteriology · 2002Article
- Stability and subcellular localization of cytadherence-associated protein P65 in Mycoplasma pneumoniae.Journal of bacteriology · 2001Article
- Stability of Mycoplasma pneumoniae cytadherence-accessory protein HMW1 correlates with its association with the triton shell.Journal of bacteriology · 2001Article
- Visualization of the attachment organelle and cytadherence proteins of Mycoplasma pneumoniae by immunofluorescence microscopy.Journal of bacteriology · 2001Article
- Transcriptional analysis of the hmw gene cluster of Mycoplasma pneumoniae.Journal of bacteriology · 1999Article
- Identification and complementation of frameshift mutations associated with loss of cytadherence in Mycoplasma pneumoniae.Journal of bacteriology · 1999Article
Corrections and comments
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Authors and funding
2 authors at 1 institution in 1 country.
Funding
Abstract
The location of the cytadherence-accessory high-molecular weight proteins 1 and 4 (HMW1/4) within Mycoplasma pneumoniae cells has been studied by both biochemical and electron microscopic techniques. Peptide mapping studies demonstrated that HMW1/4 share almost identical peptide profiles, suggesting that the two proteins are structurally related. Examination of thin sections of M. pneumoniae with antibodies to HMW1/4 and colloidal gold particles revealed distinct labeling of the filamentous extensions of the mycoplasma cells. Labeling was absent on thin sections of a cytadherence-deficient variant lacking HMW1/4. HMW1/4 partitioned in the detergent-insoluble fraction following Triton X-100 extraction, and analysis by sucrose density gradient centrifugation suggested that HMW1/4 are part of a high-molecular-weight, multiprotein complex. These results were confirmed by immunogold labeling of Triton X-100-extracted M. pneumoniae cells incubated with antibodies to HMW1/4: gold particles bound in specific clusters to detergent-insoluble filaments. Finally, immunogold labeling of whole cells revealed that HMW1/4 are exposed on the cell surface, although to a lesser degree than on the cell interior. These findings indicate that HMW1/4 are membrane proteins associated with the cytoskeletonlike triton shell of M. pneumoniae and localized primarily in the filamentous extensions of the mycoplasma cells.
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