Roy S.,Bose Institute of India |
Roy S.,University of Burdwan |
Banerjee V.,Bose Institute of India |
Banerjee V.,National Institute for Biotechnology in the Negev |
Das K.P.,Bose Institute of India
PLoS ONE | Year: 2015
Here, we have investigated the physical and molecular basis of stability of Arabidopsis DNA Pol λ, the sole X family DNA polymerase member in plant genome, under UV-B and salinity stress in connection with the function of the N-terminal BRCT (breast cancer-associated C terminus) domain and Ser-Pro rich region in the regulation of the overall structure of this protein. Tryptophan fluorescence studies, fluorescence quenching and Bis-ANS binding experiments using purified recombinant full length Pol λ and its N-terminal deletion forms have revealed UV-B induced conformational change in BRCT domain deficient Pol λ. On the other hand, the highly conserved C-terminal catalytic core PolX domain maintained its tertiary folds under similar condition. Circular dichroism (CD) and fourier transform infrared (FT-IR) spectral studies have indicated appreciable change in the secondary structural elements in UV-B exposed BRCT domain deficient Pol λ. Increased thermodynamic stability of the C-terminal catalytic core domain suggested destabilizing effect of the N-terminal Ser- Pro rich region on the protein structure. Urea-induced equilibrium unfolding studies have revealed increased stability of Pol λ and its N-terminal deletion mutants at high NaCl concentration. In vivo aggregation studies using transient expression systems in Arabidopsis and tobacco indicated possible aggregation of Pol λ lacking the BRCT domain. Immunoprecipitation assays revealed interaction of Pol λ with the eukaryotic molecular chaperone HSP90, suggesting the possibility of regulation of Pol λ stability by HSP90 in plant cell. Overall, our results have provided one of the first comprehensive information on the biophysical characteristics of Pol λ and indicated the importance of both BRCT and Ser-Pro rich modules in regulating the stability of this protein under genotoxic stress in plants. Copyright: © 2015 Roy et al. This is an open access article distributed under the terms of the Creative Commons Attribution License, which permits unrestricted use, distribution, and reproduction in any medium, provided the original author and source are credited.
Feinstein Y.,Pediatric Endocrinology Unit |
Yerushalmi B.,Pediatric Gastroeneterology Unit |
Loewenthal N.,Pediatric Endocrinology Unit |
Alkrinawi S.,Pediatric Pulmonology Unit |
And 4 more authors.
Hormone Research in Paediatrics | Year: 2014
Introduction: We identified patients of Bedouin origin with a mutation in carbonic anhydrase XII (CA XII) leading to hyponatremia due to excessive salt loss via sweat. Methods: The medical records of patients were reviewed for clinical and laboratory data. Results: A total of 11 subjects were identified; 7 symptomatic patients presented with hyponatremic dehydration in infancy. Screening of the entire kindred identified 4 asymptomatic individuals with elevated sweat chloride. All symptomatic patients had failure to thrive and moderate-severe hyponatremia (106-124 mmol·l-1); 6 had hypochloremia (79-94 mmol·l-1). All asymptomatic subjects had normal or near-normal serum sodium and chloride concentrations. Both symptomatic and asymptomatic subjects had normal renal functions and normal cortisol response on low-dose ACTH test. All symptomatic patients were treated by dietary salt, which prevents episodes of hyponatremic dehydration and promotes growth. At follow-up, the chief complaints remained heat intolerance, accumulation of salt precipitates on the face and hyperhidrosis. No evidence for chronic renal, respiratory, gastrointestinal or fertility abnormalities was found. Conclusion: Recognizing this newly described entity and differentiating it from cystic fibrosis and pseudohypoaldosteronism are important. Patients with CA XII mutations should be followed even after early childhood, especially in hot temperatures and intense physical activity. © 2014 S. Karger AG, Basel.
Home > Press > Novel anti-biofilm nano coating developed at Ben-Gurion U.: Offers significant anti-adhesive potential for a variety of medical and industrial applications Abstract: Researchers at Ben-Gurion University of the Negev (BGU) have developed an innovative anti-biofilm coating, which has significant anti-adhesive potential for a variety of medical and industrial applications. According to the research published in Advanced Materials Interfaces, anti-adhesive patches that are developed from naturally occurring biomaterials can prevent destructive bacterial biofilm from forming on metal surfaces when they are immersed in water and other damp environments. "Our solution addresses a pervasive need to design environmentally friendly materials to impede dangerous surface bacteria growth," the BGU researchers from the Avram and Stella Goldstein-Goren Department of Biotechnology Engineering explain. "This holds tremendous potential for averting biofilm formed by surface-anchored bacteria and could have a tremendous impact." The anti-adhesive could be used on medical implants, devices and surgical equipment where bacteria can contribute to chronic diseases, resist antibiotic treatment and thereby compromise the body's defense system. The prevention of aquatic biofouling on ships and bridges is one of the industrial applications. is. ### The BGU researchers who participated in the study from the Avram and Stella Goldstein-Goren Department of Biotechnology Engineering are Dr. Karina Goldberg, Prof. Noa Emuna, Prof. Dorit van Moppes, Prof. T. P. Vinod, Prof. Robert Marks, Prof. Ariel Kushmaro, and Prof. Shoshana Malis Arad. Profs. Marks and Kushmaro are members of BGU's Ilse Katz Institute for Nanoscale Science and Technology and the National Institute for Biotechnology in the Negev, and are also visiting researchers at the School of Materials Science and Engineering, Nanyang Technological University in Singapore. This work was supported by the Singapore National Research Foundation under the CREATE program: Nanomaterials for Energy and Water Management; a Levi Eshkol scholarship from the Israeli Ministry of Science and Technology, and by a Shimona Geresh award. For more information, please click If you have a comment, please us. Issuers of news releases, not 7th Wave, Inc. or Nanotechnology Now, are solely responsible for the accuracy of the content.
Gur E.,Ben - Gurion University of the Negev |
Gur E.,National Institute for Biotechnology in the Negev |
Vishkautzan M.,Ben - Gurion University of the Negev |
Vishkautzan M.,National Institute for Biotechnology in the Negev |
Sauer R.T.,Massachusetts Institute of Technology
Protein Science | Year: 2012
AAA+ proteases employ a hexameric ring that harnesses the energy of ATP binding and hydrolysis to unfold native substrates and translocate the unfolded polypeptide into an interior compartment for degradation. What determines the ability of different AAA+ enzymes to unfold and thus degrade different native protein substrates is currently uncertain. Here, we explore the ability of the E. coli Lon protease to unfold and degrade model protein substrates beginning at N-terminal, C-terminal, or internal degrons. Lon has historically been viewed as a weak unfoldase, but we demonstrate robust and processive unfolding/degradation of some substrates with very stable protein domains, including mDHFR and titin I27. For some native substrates, Lon is a more active unfoldase than related AAA+ proteases, including ClpXP and ClpAP. For other substrates, this relationship is reversed. Thus, unfolding activity does not appear to be an intrinsic enzymatic property. Instead, it depends on the specific protease and substrate, suggesting that evolution has diversified rather than optimized the protein unfolding activities of different AAA+ proteases. Published by Wiley-Blackwell. © 2011 The Protein Society.
Mandabi A.,National Institute for Biotechnology in the Negev |
Ganin H.,National Institute for Biotechnology in the Negev |
Meijler M.M.,National Institute for Biotechnology in the Negev
Bioorganic and Medicinal Chemistry Letters | Year: 2015
Abstract Autoinducer-2 (AI-2) has been suggested to serve as a ubiquitous quorum sensing (QS) signal that mediates intra- and interspecies cross-talk between bacteria. To add tools for the study of its function in bacterial communication, we present a new and an improved synthetic route to AI-2 and aromatic analogues. We used this strategy to prepare naphthyl-DPD, and observed remarkably high synergistic activity at low nanomolar concentrations for this analogue in Vibrio harveyi. © 2015 Elsevier Ltd.