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NAC in Abiotic Stresses
Published in Hasanuzzaman Mirza, Nahar Kamrun, Fujita Masayuki, Oku Hirosuke, Tofazzal M. Islam, Approaches for Enhancing Abiotic Stress Tolerance in Plants, 2019
Sami Ullah Jan, Muhammad Jamil, Muhammad Faraz Bhatti, Alvina Gul
DNA-binding domains are the primary sites for DNA–protein interactions. The part of transcription factor that has a conserved structural motif with capability to bind specific promoter or enhancer-sequence in a gene is called DNA-binding domain while, alternatively, the position/site on DNA where a transcription factor binds refers to Transcription Factor Binding Site (TFBS) or Response Element (RE) (Reid et al. , 2010). DBDs show more conserved pattern as compared to the other structural motifs (Atkinson and Urwin, 2012; Guo et al., 2005). DBDs are the key sites in determining the specificity, type and rate of binding a transcription factor to specific loci in DNA (Reid et al., 2010). These are highly organized folded-motifs with a variable number of amino acids, such as 50 in MYB-type TFs, 60 in WRKY-Type TFs (Liu et al., 2013), while 150–160 in NAC (Ooka et al., 2003).
Molecular Analysis in Mechanobiology
Published in Jiro Nagatomi, Eno Essien Ebong, Mechanobiology Handbook, 2018
Antibodies are proteins expressed by B lymphocytes that contribute to specific immune responses by binding to foreign (nonself) molecules termed antigens. The basic antibody subunit is a Y-shaped structure that is composed of two identical copies of heavy and light chains connected by disulfide bridges (Figure 3.4). Five different classes of antibodies are expressed (IgM, IgG, IgD, IgA, and IgE) that differ in the number of Y subunits and the type of heavy chain. Each antibody subunit has two antigen-binding domains in the Fab regions that are identical among all the antibodies produced by an individual B cell, but highly variable among the overall population of B cells. This diversity results from recombination of the immunoglobulin genes during B cell maturation and provides each individual with an antibody repertoire capable of recognizing an estimated >109 different antigens [66]. Each antibody subunit also has an Fc region that is constant among all the antibodies of a particular class and provides binding sites for complement proteins and macrophages. The antigen-binding domains of each antibody recognize a relatively small region of the antigen (typically 6–10 amino acids) termed an epitope. Therefore, a typical antigen such as a protein will contain multiple epitopes, each of which may be recognized by different specific antibodies. Antibody–antigen binding is mediated by multiple, cooperative non-covalent interactions, providing very high specificity that has made antibodies the central tool for studying protein expression.
Understanding the Technologies Involved in Gene Therapy
Published in Yashwant V. Pathak, Gene Delivery Systems, 2022
Manish P. Patel, Jayvadan K. Patel, Mukesh Patel, Govind Vyas
Research was carried out on bacterial plant pathogen Xanthomonads which causes diseases on many plants a by Hrp-type III secretion (T3S) system. This secretion system is key in the translocation of effector proteins inside plant cells. It was also noted that the effector has a wide role in supporting bacterial virulence, multiplication and distribution. AvrBs3 or transcription activator-like (TAL) localized on pXV11 group (h2) genes were found in a significant amount in Xanthomonas spp. As the name suggests, TAL activates transcription in the cell nucleus. The binding specificity is determined by a modular DNA-binding domain (Boch et al. 2010).
Enolase, a cadmium resistance related protein from hyperaccumulator plant Phytolacca americana, increase the tolerance of Escherichia coli to cadmium stress
Published in International Journal of Phytoremediation, 2023
Le Zhao, Yunhao Zhu, Min Wang, Yongguang Han, Jiao Xu, Weisheng Feng, Xiaoke Zheng
In human cells, HsENO1 (α-enolase) gene can be translated into the transcription factor MBP-1 from the second start codon ATG (amino acid 94). The same phenomenon was also found in A. thaliana, where AtENO2 (LOS2) gene can be translated into AtMBP-1 from the second start codon (amino acid 93) (Figure S4a). The MBP-1 protein was a transcription factor that contained a DNA binding domain and a transcriptional repression domain (Figure S4a). Sequence alignment of PaENO with HsENO1 and AtENO2 revealed that PaENO also contained DNA binding and transcriptional repression domains, so PaENO may have transcription factor activity (Figure S4b). By constructing the prokaryotic expression vector, it was found that the expression of PaMBP-1 enhanced the resistance of E. coli to Cd (Figure S4c,d). These results indicated that the expression of PaENO increased the tolerance of E. coli to Cd, which may be achieved through the alternative translation of PaENO into the transcription factor PaMBP-1.
Straightforward sustainable synthesis of novel non-endocrine disruptive bio-based organic UV-B filters with antimicrobial activity
Published in Green Chemistry Letters and Reviews, 2023
Matthieu M. Mention, Cédric Peyrot, Blandine Godon, Jimmy Alarcan, Fanny Brunissen, Marina Grimaldi, Patrick Balaguer, Albert Braeuning, Florent Allais
To characterize the ERα, AR, TRα and TRβ activities, we used already established HELN hERα, U2OS hAR, HG5LN rTRα and HG5LN rTRβ reporter cell lines (22–24). Briefly, HELN hERα cells were obtained by stably expression of human ER αin HELN (HeLa ERE-luciferase) cells whereas to characterize the AR activity, U2OS cells were stably co-transfected with a androgen responsive gene, ARE(Rad9)-collagenase-Luc-hygromycin, and a human AR expressing plasmid. Finally, HG5LN rTRα and HG5LN rTRβ cells were obtained by stably expression of individual ligand binding domains of rat TRα and TRβ fused to GAL4 DNA binding domain in HG5LN (HeLa GAL4REx5 – luciferase) cells. HELN ERα cells were cultured in Dulbecco's Modified Eagle Medium: Nutrient Mixture F-12 (DMEM/F-12) without phenol red and 1 g/L glucose and supplemented with 5% stripped fetal bovine serum, 100 units/mL of penicillin, 100 μg/mL of streptomycin, 0.5 μg/mL puromycin and 1 mg/mL geneticin in a 5% CO2 humidified atmosphere at 37°C. HG5LN rTRα and rTRβ cells were cultured in Dulbecco's Modified Eagle Medium: Nutrient Mixture F-12 (DMEM/F-12) containing phenol red and 1 g/L glucose and supplemented with 5% fetal bovine serum, 100 units/mL of penicillin, 100 μg/mL of streptomycin, 0.5 μg/mL puromycin and 1 mg/mL geneticin in a 5% CO2 humidified atmosphere at 37°C. U2OS hAR cells were cultured in the same medium supplemented with hygromycin 0.25 mg/mL.
An update on COVID-19: SARS-CoV-2 life cycle, immunopathology, and BCG vaccination
Published in Preparative Biochemistry & Biotechnology, 2021
Shankar M. Khade, Shivraj M. Yabaji, Jyoti Srivastava
Elucidation of the structure of coronavirus would help in understanding the possible targets and mechanisms of action of different drugs for treatment purposes. Coronaviridae family consists of enveloped viruses containing positive single-stranded RNA (+ssRNA) as a genome, which is linear, non-segmented. The coronavirus consists of three structural proteins—the nucleocapsid protein N, which is integrated with the genome. The viral nucleoprotein is protected by the lipid bilayer membrane staggered with the glycoproteins which present as an integral membrane protein that spans the lipid bilayer and the outer peplomer protein as shown in Figure 1.[33] The genomic sequencing of the COVID-19 delineated the close relationship of about 88% to that of the two bat viruses bat-SL-CoVZC45 and bat-SL-CoVXC21, but the match was more distant from SARS-CoV (∼79%) and to that of MERS-CoV (∼50%). However, the 2009-nCoV possesses a similar kind of receptor-binding domain structure with that of SARS-CoV. The phylogenetic analysis has revealed the primary host of the SARS-CoV-2 is bats, which has been transmitted to the human via some intermediate animal.[34]