scholarly journals AnabaenaFlavodoxin as an Electron Carrier from Photosystem I to Ferredoxin-NADP+Reductase. Role of Flavodoxin Residues in Protein−Protein Interaction and Electron Transfer†

Biochemistry ◽  
2005 ◽  
Vol 44 (1) ◽  
pp. 97-104 ◽  
Author(s):  
Isabel Nogués ◽  
Manuel Hervás ◽  
José R. Peregrina ◽  
José A. Navarro ◽  
Miguel A. de la Rosa ◽  
...  
Keyword(s):  
Electron Transfer ◽  
Photosystem I ◽  
Protein Interaction ◽  
Electron Carrier ◽  
Protein Protein Interaction

scholarly journals Dual role of FMN in flavodoxin function: Electron transfer cofactor and modulation of the protein–protein interaction surface

2010 ◽  
Vol 1797 (2) ◽  
pp. 262-271 ◽  
Author(s):  
Susana Frago ◽  
Isaias Lans ◽  
José A. Navarro ◽  
Manuel Hervás ◽  
Dale E. Edmondson ◽  
...  
Keyword(s):  
Electron Transfer ◽  
Protein Interaction ◽  
Dual Role ◽  
Protein Protein Interaction ◽  
Interaction Surface

scholarly journals Regulation of clathrin coat assembly by Eps15 homology domain–mediated interactions during endocytosis

2012 ◽  
Vol 23 (4) ◽  
pp. 687-700 ◽  
Author(s):  
Ryohei Suzuki ◽  
Junko Y. Toshima ◽  
Jiro Toshima
Keyword(s):  
Functional Diversity ◽  
Protein Interaction ◽  
Interaction Domain ◽  
Protein Protein Interaction ◽  
Molecular Events ◽  
Biological Studies ◽  
Eh Domain ◽  
Actin Patch ◽  
Lines Of Evidence

Clathrin-mediated endocytosis involves a coordinated series of molecular events regulated by interactions among a variety of proteins and lipids through specific domains. One such domain is the Eps15 homology (EH) domain, a highly conserved protein–protein interaction domain present in a number of proteins distributed from yeast to mammals. Several lines of evidence suggest that the yeast EH domain–containing proteins Pan1p, End3p, and Ede1p play important roles during endocytosis. Although genetic and cell-biological studies of these proteins suggested a role for the EH domains in clathrin-mediated endocytosis, it was unclear how they regulate clathrin coat assembly. To explore the role of the EH domain in yeast endocytosis, we mutated those of Pan1p, End3p, or Ede1p, respectively, and examined the effects of single, double, or triple mutation on clathrin coat assembly. We found that mutations of the EH domain caused a defect of cargo internalization and a delay of clathrin coat assembly but had no effect on assembly of the actin patch. We also demonstrated functional redundancy among the EH domains of Pan1p, End3p, and Ede1p for endocytosis. Of interest, the dynamics of several endocytic proteins were differentially affected by various EH domain mutations, suggesting functional diversity of each EH domain.

scholarly journals Analysis of origin and protein-protein interaction maps suggests distinct oncogenic role of nuclear EGFR during cancer evolution

2017 ◽  
Vol 8 (5) ◽  
pp. 903-912 ◽  
Author(s):  
Ainur Sharip ◽  
Diyora Abdukhakimova ◽  
Xiao Wang ◽  
Alexey Kim ◽  
Yevgeniy Kim ◽  
...  
Keyword(s):  
Protein Interaction ◽  
Cancer Evolution ◽  
Protein Protein Interaction

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 Essential Role of a Single Arginine of Photosystem I in Stabilizing the Electron Transfer Complex with Ferredoxin

2000 ◽  
Vol 275 (10) ◽  
pp. 7030-7036 ◽  
Author(s):  
Patrick Barth ◽  
Isabelle Guillouard ◽  
Pierre Sétif ◽  
Bernard Lagoutte
Keyword(s):  
Electron Transfer ◽  
Photosystem I ◽  
Essential Role ◽  
Electron Transfer Complex
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