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Palmitoylated proteins in Ureaplasma urealyticum
D Thirkell1, A D Myles, W C Russell
1Department of Biochemistry and Microbiology, University of St. Andrews, Fife Scotland.
Infection and Immunity
|March 1, 1991
Summary
This study reveals that Ureaplasma urealyticum serotype 8 proteins are acylated, with many associated with the cell membrane. These findings shed light on the bacterium
Area of Science:
- Microbiology
- Molecular Biology
- Biochemistry
Background:
- Ureaplasma urealyticum is a common human pathogen.
- Understanding its protein modifications is crucial for pathogen research.
Purpose of the Study:
- To investigate protein acylation in Ureaplasma urealyticum serotype 8.
- To identify acylated proteins and determine their cellular localization.
Main Methods:
- Incubation with 3H-labeled palmitic acid.
- Electrophoresis and fluorography to detect acylated proteins.
- Immunoprecipitation to identify antigenic proteins.
- Triton X-114 phase partition to assess amphipathicity and membrane association.
Main Results:
- Approximately 25 acylated proteins were detected in Ureaplasma urealyticum serotype 8.
- At least six acylated proteins were antigenic, including the 96-kDa surface antigen.
- The 96-kDa antigen and other acylated proteins preferentially partitioned into the detergent phase, indicating amphipathic properties.
- Results suggest most acylated proteins are membrane-associated.
Conclusions:
- Protein acylation is a significant post-translational modification in Ureaplasma urealyticum serotype 8.
- The 96-kDa surface antigen is acylated and likely membrane-associated.
- Acylated proteins play a role in the bacterium's structure and function, potentially in membrane association.