Novel insight into mutational impacts and binding mechanism of human glutaminase and glutaminase-interacting protein: A bio-molecular modeling and docking analysis

Gene Reports ◽  
2017 ◽  
Vol 8 ◽  
pp. 49-60
Author(s):  
Arundhati Banerjee ◽  
Sujay Ray
2015 ◽  
Vol 29 (3) ◽  
pp. 248-262 ◽  
Author(s):  
Vladimir Vukić ◽  
Dajana Hrnjez ◽  
Spasenija Milanović ◽  
Mirela Iličić ◽  
Katarina Kanurić ◽  
...  

2015 ◽  
Vol 99 (21) ◽  
pp. 8917-8925 ◽  
Author(s):  
Prakram Singh Chauhan ◽  
Satya Prakash Tripathi ◽  
Abhays T. Sangamwar ◽  
Neena Puri ◽  
Prince Sharma ◽  
...  

Genetics ◽  
2002 ◽  
Vol 162 (2) ◽  
pp. 633-645 ◽  
Author(s):  
Guido Cuperus ◽  
David Shore

Abstract We previously described two classes of SIR2 mutations specifically defective in either telomeric/HM silencing (class I) or rDNA silencing (class II) in S. cerevisiae. Here we report the identification of genes whose protein products, when either overexpressed or directly tethered to the locus in question, can establish silencing in SIR2 class I mutants. Elevated dosage of SCS2, previously implicated as a regulator of both inositol biosynthesis and telomeric silencing, suppressed the dominant-negative effect of a SIR2-143 mutation. In a genetic screen for proteins that restore silencing when tethered to a telomere, we isolated ESC2 and an uncharacterized gene, (YOL017w), which we call ESC8. Both Esc2p and Esc8p interact with Sir2p in two-hybrid assays, and the Esc8p-Sir2 interaction is detected in vitro. Interestingly, Esc8p has a single close homolog in yeast, the ISW1-complex factor Ioc3p, and has also been copurified with Isw1p, raising the possibility that Esc8p is a component of an Isw1p-containing nucleosome remodeling complex. Whereas esc2 and esc8 deletion mutants alone have only marginal silencing defects, cells lacking Isw1p show a strong silencing defect at HMR but not at telomeres. Finally, we show that Esc8p interacts with the Gal11 protein, a component of the RNA pol II mediator complex.


2016 ◽  
Vol 113 (11) ◽  
pp. 3042-3047 ◽  
Author(s):  
Elena Del Tordello ◽  
Olga Danilchanka ◽  
Andrew J. McCluskey ◽  
John J. Mekalanos

The bacterial type 6 secretion system (T6SS) is a dynamic apparatus that translocates proteins between cells by a mechanism analogous to phage tail contraction. T6SS sheaths are cytoplasmic tubular structures composed of stable VipA-VipB (named for ClpV-interacting protein A and B) heterodimers. Here, the structure of the VipA/B sheath was exploited to generate immunogenic multivalent particles for vaccine delivery. Sheaths composed of VipB and VipA fused to an antigen of interest were purified from Vibrio cholerae or Escherichia coli and used for immunization. Sheaths displaying heterologous antigens generated better immune responses against the antigen and different IgG subclasses compared with soluble antigen alone. Moreover, antigen-specific antibodies raised against sheaths presenting Neisseria meningitidis factor H binding protein (fHbp) antigen were functional in a serum bactericidal assay. Our results demonstrate that multivalent nanoparticles based on the T6SS sheath represent a versatile scaffold for vaccine applications.


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