scholarly journals Bradykinin B2 receptor signaling: Structural and functional characterization of the C-terminus

Biopolymers ◽  
2005 ◽  
Vol 80 (2-3) ◽  
pp. 367-373 ◽  
Author(s):  
Andrea Piserchio ◽  
Veronica Zelesky ◽  
Jun Yu ◽  
Linda Taylor ◽  
Peter Polgar ◽  
...  
Keyword(s):  
Functional Characterization ◽  
Receptor Signaling ◽  
Bradykinin B2 Receptor ◽  
C Terminus

scholarly journals Functional Characterization of the Interaction of Ste50p with Ste11p MAPKKK inSaccharomyces cerevisiae

1999 ◽  
Vol 10 (7) ◽  
pp. 2425-2440 ◽  
Author(s):  
Cunle Wu ◽  
Ekkehard Leberer ◽  
David Y. Thomas ◽  
Malcolm Whiteway
Keyword(s):  
Protein Kinase ◽  
Functional Characterization ◽  
Hog Pathway ◽  
C Terminus ◽  
Extracellular Signal ◽  
Osmotic Stress Response ◽  
N Terminus

The Saccharomyces cerevisiae Ste11p protein kinase is a homologue of mammalian MAPK/extracellular signal-regulated protein kinase kinase kinases (MAPKKKs or MEKKs) as well as theSchizosaccharomyces pombe Byr2p kinase. Ste11p functions in several signaling pathways, including those for mating pheromone response and osmotic stress response. The Ste11p kinase has an N-terminal domain that interacts with other signaling molecules to regulate Ste11p function and direct its activity in these pathways. One of the Ste11p regulators is Ste50p, and Ste11p and Ste50p associate through their respective N-terminal domains. This interaction relieves a negative activity of the Ste11p N terminus, and removal of this negative function is required for Ste11p function in the high-osmolarity glycerol (HOG) pathway. The Ste50p/Ste11p interaction is also important (but not essential) for Ste11p function in the mating pathway; in this pathway binding of the Ste11p N terminus with both Ste50p and Ste5p is required, with the Ste5p association playing the major role in Ste11p function. In vitro, Ste50p disrupts an association between the catalytic C terminus and the regulatory N terminus of Ste11p. In addition, Ste50p appears to modulate Ste11p autophosphorylation and is itself a substrate of the Ste11p kinase. Therefore, both in vivo and in vitro data support a role for Ste50p in the regulation of Ste11p activity.

scholarly journals Purification and Functional Characterization of the C-Terminal Domain of the β-Actin-Binding Protein AIM1 In Vitro

Molecules ◽  
2018 ◽  
Vol 23 (12) ◽  
pp. 3281 ◽  
Author(s):  
Fang Wu ◽  
Liangkai Cheng ◽  
Qi Yu ◽  
Lin Zhang ◽  
Hong Li ◽  
...  
Keyword(s):  
Prostate Cancer ◽  
Structural Model ◽  
Functional Characterization ◽  
Actin Binding ◽  
Migration And Invasion ◽  
Binding Modes ◽  
C Terminus ◽  
Biology Research

The protein absent in melanoma 1 (AIM1) is a member of the βγ-crystal lens superfamily that is associated with the development of multiple cancers. The binding of AIM1 to β-actin affects the migration and invasion of prostate cancer epithelial cells. The C-terminus of AIM1 is required for the β-actin interaction. However, the characteristics of AIM1 in vitro and the interaction mode between AIM1 and β-actin remain unknown. We describe novel methods to prepare pure recombinant AIM1 and identify possible binding modes between AIM1 and β-actin; we also obtain the crystal of the first two βγ-crystallin domains of AIM1 (g1g2) for future structural biology research. We first express and purify AIM1 after cloning the sequence into a modified pET-28a_psp expression vector. Next, we define the minimum unit formed by the βγ-crystallin domain repeats that bound to β-actin and perform its physiological function. Finally, we made the structural model of the AIM1 g1g2 that can be used to guide future biomedical investigations and prostate cancer research.

scholarly journals Functional characterization of FlgM in the regulation of flagellar synthesis and motility in Yersinia pseudotuberculosis

Microbiology ◽  
2009 ◽  
Vol 155 (6) ◽  
pp. 1890-1900 ◽  
Author(s):  
Lisha Ding ◽  
Yao Wang ◽  
Yangbo Hu ◽  
Steve Atkinson ◽  
Paul Williams ◽  
...  
Keyword(s):  
Yersinia Pseudotuberculosis ◽  
Functional Characterization ◽  
Direct Interaction ◽  
Site Directed Mutagenesis ◽  
Wild Type ◽  
C Terminus ◽  
In Trans ◽  
Differential Gene ◽  
Flagellar Biogenesis

We describe here the functional characterization of the flgM gene in Yersinia pseudotuberculosis. Direct interaction of FlgM with the alternative sigma factor σ 28 (FliA) was first confirmed. A conserved region in the C-terminus of FlgM was found which included the σ 28 binding domain. By site-directed mutagenesis, bacterial two-hybrid analysis and Western blotting, the primary FlgM binding sites with σ 28 were shown to be Ile85, Ala86 and Leu89. A role for FlgM in swimming motility was demonstrated by inactivation of flgM and subsequent complementation in trans. Transcriptional fusion analyses showed differential gene expression of flhDC, fliA, flgM and fliC in the fliA and flgM mutants compared with the wild-type. flhDC expression was not influenced by σ 28 or FlgM while fliA expression was abolished in the fliA mutant and considerably reduced in the flgM mutant when compared to the wild-type, indicating that both FliA and FlgM can activate fliA transcription. Conversely, flgM transcription was higher in the fliA mutant when compared to the wild-type, suggesting that flgM transcription was repressed by σ 28. Interestingly, fliC expression was markedly increased in the flgM mutant, suggesting a negative regulatory role for FlgM in fliC expression. The transcription of other σ-dependent genes (cheW, flgD, flaA, csrA and fliZ) was also examined in fliA and flgM mutant backgrounds and this revealed that other σ-factors apart from σ 28 may be involved in flagellar biogenesis in Y. pseudotuberculosis. Taking together the motility phenotypes and effects of flgM mutation on the regulation of these key motility genes, we propose that the mechanisms regulating flagellar biogenesis in Y. pseudotuberculosis may differ from those described for other bacteria.

scholarly journals Functional Characterization of a Novel Frameshift Mutation in the C-terminus of the Nav1.5 Channel Underlying a Brugada Syndrome with Variable Expression in a Spanish Family

PLoS ONE ◽  
2013 ◽  
Vol 8 (11) ◽  
pp. e81493 ◽  
Author(s):  
Pablo Dolz-Gaitón ◽  
Mercedes Núñez ◽  
Lucía Núñez ◽  
Adriana Barana ◽  
Irene Amorós ◽  
...  
Keyword(s):  
Brugada Syndrome ◽  
Frameshift Mutation ◽  
Functional Characterization ◽  
Variable Expression ◽  
C Terminus ◽  
Spanish Family

scholarly journals Functional Characterization of FLT3 Receptor Signaling Deregulation in Acute Myeloid Leukemia by Single Cell Network Profiling (SCNP)

PLoS ONE ◽  
2010 ◽  
Vol 5 (10) ◽  
pp. e13543 ◽  
Author(s):  
David B. Rosen ◽  
Mark D. Minden ◽  
Steven M. Kornblau ◽  
Aileen Cohen ◽  
Urte Gayko ◽  
...  
Keyword(s):  
Acute Myeloid Leukemia ◽  
Single Cell ◽  
Myeloid Leukemia ◽  
Functional Characterization ◽  
Receptor Signaling ◽  
Cell Network ◽  
Acute Myeloid

scholarly journals Characterization of a UDP-N-acetyl-D-galactosamine:polypeptide N-acetylgalactosaminyltransferase with an unusual lectin domain from the platyhelminth parasite Echinococcus granulosus

2004 ◽  
Vol 382 (2) ◽  
pp. 501-510 ◽  
Author(s):  
Teresa FREIRE ◽  
Cecilia FERNÁNDEZ ◽  
Cora CHALAR ◽  
Rick M. MAIZELS ◽  
Pedro ALZARI ◽  
...  
Keyword(s):  
Echinococcus Granulosus ◽  
Transmembrane Domain ◽  
Functional Characterization ◽  
Maximal Activity ◽  
Structural Features ◽  
Helminth Parasites ◽  
Lectin Domain ◽  
C Terminus ◽  
The One

As part of a general project aimed at elucidating the initiation of mucin-type O-glycosylation in helminth parasites, we have characterized a novel ppGalNAc-T (UDP-N-acetyl-D-galactosamine:polypeptide N-acetylgalactosaminyltransferase) from the cestode Echinococcus granulosus (Eg-ppGalNAc-T1). A full-length cDNA was isolated from a library of the tissue-dwelling larval stage of the parasite, and found to code for a 654-amino-acid protein containing all the structural features of ppGalNAc-Ts. Functional characterization of a recombinant protein lacking the transmembrane domain showed maximal activity at 28 °C, in the range 6.5–7.5 pH units and in the presence of Cu2+. In addition, it transferred GalNAc to a broad range of substrate peptides, derived from human mucins and O-glycosylated parasite proteins, including acceptors containing only serine or only threonine residues. Interestingly, the C-terminal region of Eg-ppGalNAc-T1 bears a highly unusual lectin domain, considerably longer than the one from other members of the family, and including only one of the three ricin B repeats generally present in ppGalNAc-Ts. Furthermore, a search for conserved domains within the protein C-terminus identified a fragment showing similarity to a recently defined domain, specialized in the binding of organic phosphates (CYTH). The role of the lectin domain in the determination of the substrate specificity of these enzymes suggests that Eg-ppGalNAc-T1 would be involved in the glycosylation of a special type of substrate. Analysis of the tissue distribution by in situ hybridization and immunohistochemistry revealed that this transferase is expressed in the hydatid cyst wall and the subtegumental region of larval worms. Therefore it could participate in the biosynthesis of O-glycosylated parasite proteins exposed at the interface between E. granulosus and its hosts.

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