ProteoChip: A highly sensitive protein microarray prepared by a novel method of protein immobilization for application of protein-protein interaction studies

PROTEOMICS ◽  
2003 ◽  
Vol 3 (12) ◽  
pp. 2289-2304 ◽  
Author(s):  
Yoonsuk Lee ◽  
Eun Kyoung Lee ◽  
Yong Wan Cho ◽  
Takuya Matsui ◽  
In-Cheol Kang ◽  
...  
Keyword(s):  
Protein Interaction ◽  
Protein Microarray ◽  
Protein Immobilization ◽  
Protein Protein Interaction ◽  
Interaction Studies ◽  
Highly Sensitive ◽  
Novel Method

scholarly journals Definition of a minimal munc18c domain that interacts with syntaxin 4

2000 ◽  
Vol 350 (3) ◽  
pp. 741-746 ◽  
Author(s):  
Julian GRUSOVIN ◽  
Violet STOICHEVSKA ◽  
Keith H. GOUGH ◽  
Katrina NUNAN ◽  
Colin W. WARD ◽  
...  
Keyword(s):  
Protein Interaction ◽  
Full Length ◽  
Yeast Two Hybrid ◽  
Protein Protein Interaction ◽  
Interaction Studies ◽  
Syntaxin 4 ◽  
Definition Of ◽  
Two Hybrid

munc18c is a critical protein involved in trafficking events associated with syntaxin 4 and which also mediates inhibitory effects on vesicle docking and/or fusion. To investigate the domains of munc18c responsible for its interaction with syntaxin 4, fragments of munc18c were generated and their interaction with syntaxin 4 examined in vivo by the yeast two-hybrid assay. In vitro protein–protein interaction studies were then used to confirm that the interaction between the proteins was direct. Full-length munc18c1–592, munc18c1–139 and munc18c1–225, but not munc18c226–592, munc18c1–100, munc18c43–139 or munc18c66–139, interacted with the cytoplasmic portion of syntaxin 4, Stx42–273, as assessed by yeast two-hybrid assay of growth on nutritionally deficient media and by β-galactosidase reporter induction. The N-terminal predicted helix-a-helix-b-helix-c region of syntaxin 4, Stx429–157, failed to interact with full-length munc18c1–592, indicating that a larger portion of syntaxin 4 is necessary for the interaction. The yeast two-hybrid results were confirmed by protein–protein interaction studies between Stx42–273 and glutathione S-transferase fusion proteins of munc18c. Full-length munc18c1–592, munc18c1–139 and munc18c1–225 interacted with Stx42–273 whereas munc18c1–100 did not, consistent with the yeast two-hybrid data. These data thus identify a region of munc18c between residues 1 and 139 as a minimal domain for its interaction with syntaxin 4.

Potential of mean force for protein-protein interaction studies

2002 ◽  
Vol 46 (2) ◽  
pp. 190-196 ◽  
Author(s):  
Lin Jiang ◽  
Ying Gao ◽  
Fenglou Mao ◽  
Zhijie Liu ◽  
Luhua Lai
Keyword(s):  
Protein Interaction ◽  
Potential Of Mean Force ◽  
Protein Protein Interaction ◽  
Interaction Studies

scholarly journals VimA is part of the maturation pathway for the major gingipains of Porphyromonas gingivalis W83

Microbiology ◽  
2006 ◽  
Vol 152 (11) ◽  
pp. 3383-3389 ◽  
Author(s):  
E. Vanterpool ◽  
F. Roy ◽  
W. Zhan ◽  
S. M. Sheets ◽  
L. Sangberg ◽  
...  
Keyword(s):  
Gene Product ◽  
Porphyromonas Gingivalis ◽  
Protein Interaction ◽  
Protein Protein Interaction ◽  
Interaction Studies ◽  
Defective Mutant ◽  
Protease Activation ◽  
Porphyromonas Gingivalis W83

The authors have shown previously that the vimA gene, which is part of the bcp-recA-vimA operon, plays an important role in protease activation in Porphyromonas gingivalis. The gingipain RgpB proenzyme is secreted in the vimA-defective mutant P. gingivalis FLL92. An important question that is raised is whether the vimA gene product could directly interact with the proteases for their activation or regulate a pathway responsible for protease activation. To further study the mechanism(s) of VimA-dependent protease activation, the vimA gene product was further characterized. A 39 kDa protein consistent with the size of the predicted VimA protein was purified. In protein–protein interaction studies, the VimA protein was shown to interact with gingipains RgpA, RgpB and Kgp. Immune sera from mice immunized with P. gingivalis immunoreacted with the purified VimA protein. Taken together, these data suggest an interaction of VimA with the gingipains and further confirm the role of this protein in their regulation or maturation.

scholarly journals One-plasmid tunable coexpression for mycobacterial protein-protein interaction studies

2009 ◽  
Vol 18 (11) ◽  
pp. 2316-2325 ◽  
Author(s):  
Yong Chang ◽  
David Mead ◽  
Vinay Dhodda ◽  
Phil Brumm ◽  
Brian G. Fox
Keyword(s):  
Protein Interaction ◽  
Protein Protein Interaction ◽  
Interaction Studies ◽  
Mycobacterial Protein
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