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Author Aguirre, Socorro Maria, author.
Title Analysis of SNARE protein Sec22b interaction with legionella pneumophila SdhB C-terminus / by Socorro Maria Aguirre.
Published [Northridge, California] : California State University, Northridge, 2012.
LOCATION CALL # STATUS
 Electronic Book  QH51 .Z95 2012 A48eb    ONLINE
  
Description 1 online resource (vi, 67 pages) : illustrations, some color.
Content Type text
still image
Format online resource
File Characteristics text file PDF
Thesis M.S. California State University, Northridge 2012.
Bibliography Includes bibliographical references (pages 52-58).
Summary A previous yeast two-hybrid screen suggested that there was an interaction between SdhB and Sec22b, a Soluble NSF Attachment Protein REceptor (SNARE) on endoplasmic reticulum vesicles. Sec22b is involved in vesicular trafficking that takes place between the endoplasmic reticulum-Golgi intermediate compartment (ER-GIC) and the Golgi apparatus. Sec22b normally binds to three SNARES on the ER-Golgi intermediate compartment or on the Golgi apparatus. It was hypothesized that the N-terminus of SdhB interacts with the SNARE Sec22b; the regions of the N-terminus that are important for this interaction remain to be identified. To investigate potential protein-protein interactions between SdhB and Sec22b in vitro, the C-terminus portion of sdhB was cloned into a glutathione-S-transferase expression vector pGEX-5x-1 to create a protein fusion between glutatione S-transferase (GST) and SdhB. Expression of the GST-SdhB fusion protein in E. coli was optimized, and conditions for binding specific amounts of GST-SdhB from lysates cleared of cell debris onto glutathione-coated beads was determined. Beads previously coated with GST-SdhB were unable to bind His-tagged Sec22b. This was shown in both stained protein gels and by Western blotting. Sec22b was also unable to bind to GST-only controls. Similar results were obtained if Sec22b and the fusion protein underwent simultaneous incubation with the glutathione beads to control for the requirement of pre-association of proteins prior to glutathione binding. These results indicate the L. pneumophila effector protein SdhB C-terminus is not involved in a protein-protein interaction with Sec22b.
Note Description based on online resource; title from PDF title page (viewed on January 16, 2013).
Subject Legionella pneumophila -- Research.
Protein-protein interactions -- Research.
Local Subject Dissertations, Academic -- CSUN -- Biology.
Alternate Title Analysis of Soluble NSF Attachment Protein Receptor protein Sec22b interaction with legionella pneumophila SdhB C-terminus
OCLC number 847539463