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Rajat Banerjee

Bio: Rajat Banerjee is an academic researcher from University of Calcutta. The author has contributed to research in topics: Transfer RNA & Aminoacyl tRNA synthetase. The author has an hindex of 14, co-authored 23 publications receiving 661 citations. Previous affiliations of Rajat Banerjee include Bose Institute & Ohio State University.

Papers
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Journal ArticleDOI
TL;DR: The cell-free supernatant of the organism, grown with the help of shredded plastic shows the presence of the over expressed proteins with approximate molecular weight of about 55 kDa and 35 kDa, through SDS-PAGE analysis.

79 citations

Journal ArticleDOI
TL;DR: For example, the authors showed that error-prone mtPheRS, editing-deficient ctPhers, and their wild-type counterparts all supported cytoplasmic protein synthesis and cell growth and showed that the limits of translational accuracy may be largely determined by cellular physiology.
Abstract: Protein synthesis has an overall error rate of approximately 10-4 for each mRNA codon translated. The fidelity of translation is mainly determined by two events: synthesis of cognate amino acid:tRNA pairs by aminoacyl-tRNA synthetases (aaRSs) and accurate selection of aminoacyl-tRNAs (aa-tRNAs) by the ribosome. To ensure faithful aa-tRNA synthesis, many aaRSs employ a proofreading (“editing”) activity, such as phenylalanyl-tRNA synthetases (PheRS) that hydrolyze mischarged Tyr-tRNAPhe. Eukaryotes maintain two distinct PheRS enzymes, a cytoplasmic (ctPheRS) and an organellar form. CtPheRS is similar to bacterial enzymes in that it consists of a heterotetramer in which the α-subunits contain the active site and the β-subunits harbor the editing site. In contrast, mitochondrial PheRS (mtPheRS) is an α-subunit monomer that does not edit Tyr-tRNAPhe, and a comparable transacting activity does not exist in organelles. Although mtPheRS does not edit, it is extremely specific as only one Tyr-tRNAPhe is synthesized for every ∼7,300 Phe-tRNAPhe, compatible with an error rate in translation of ∼10-4. When the error rate of mtPheRS was increased 17-fold, the corresponding strain could not grow on respiratory media and the mitochondrial genome was rapidly lost. In contrast, error-prone mtPheRS, editing-deficient ctPheRS, and their wild-type counterparts all supported cytoplasmic protein synthesis and cell growth. These striking differences reveal unexpectedly divergent requirements for quality control in different cell compartments and suggest that the limits of translational accuracy may be largely determined by cellular physiology.

75 citations

Journal ArticleDOI
TL;DR: The effect of a room temperature ionic liquid (RTIL) on the conformational dynamics of a protein, human serum albumin (HSA), is studied by fluorescence correlation spectroscopy (FCS) and suggests recoiling of the unfolded protein by RTIL.
Abstract: The effect of a room temperature ionic liquid (RTIL) on the conformational dynamics of a protein, human serum albumin (HSA), is studied by fluorescence correlation spectroscopy (FCS). For this, the protein was covalently labeled by a fluorophore, 7-dimethylamino-3-(4-maleimidophenyl)-4-methylcoumarin (CPM). On addition of a RTIL ([pmim][Br]) to the native protein, the diffusion coefficient (Dt) decreases and the hydrodynamic radius (Rh) increases. This suggests that the RTIL ([pmim][Br]) acts as a denaturant when the protein is in the native state. However, addition of [pmim][Br] to a protein denatured by GdnHCl causes an increases in Dt and decrease in Rh. This suggests that in the presence of GdnHCl addition of RTIL helps the protein to refold. In the native state, the conformational dynamics of protein is described by three distinct time constants: ∼3.6 ± 0.7, ∼29 ± 4.5, and 133 ± 23 μs. The faster components (∼3.6 ± 0.7 and ∼29 ± 4.5 μs) are ascribed to chain dynamics of the protein, while the slowest...

74 citations

Journal ArticleDOI
TL;DR: A blue luminescent high-spin (s = 5/2) iron(III) complex, [FeIII(HL1)2]Cl (2), was synthesized with the acyclic tridentate salicylaldehyde 2-pyridyl hydrazone ligand, H2L1 (1), and it can subsequently be deprotonated and methylated into blue lumininescent iron( III) complexes, [ FeIII(L2)2],Cl (3), and [Fe III(MeL1) 2]Cl

70 citations

Journal ArticleDOI
TL;DR: In this article, the photophysics of the probe 4-(N-bromoacetylamino)-phthalimide (I) is dramatically different from that of the parent compound, 4-aminophthalimide.
Abstract: 4-(N-bromoacetylamino)-phthalimide (I) is used as a new solvation probe for protein and microemulsions. The photophysics of the probe 4-(N-bromoacetylamino)-phthalimide (I) is dramatically different from that of the parent compound, 4-aminophthalimide (4-AP). The solvation dynamics of I in an AOT microemulsion is similar to that of 4-AP in microemulsions. Solvation dynamics in the vicinity of a protein glutaminyl-tRNA synthetase (GlnRS) is studied by covalently attaching I to the protein. The solvation dynamics of the protein-bound probe is described by a very fast component of 40 ps and another of 580 ps.

57 citations


Cited by
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Journal ArticleDOI
TL;DR: A comprehensive review highlights recent advances in understanding of the intestinal pathotypes of E. coli, which carry an enormous potential to cause disease and continue to present challenges to human health.
Abstract: Although Escherichia coli can be an innocuous resident of the gastrointestinal tract, it also has the pathogenic capacity to cause significant diarrheal and extraintestinal diseases. Pathogenic variants of E. coli (pathovars or pathotypes) cause much morbidity and mortality worldwide. Consequently, pathogenic E. coli is widely studied in humans, animals, food, and the environment. While there are many common features that these pathotypes employ to colonize the intestinal mucosa and cause disease, the course, onset, and complications vary significantly. Outbreaks are common in developed and developing countries, and they sometimes have fatal consequences. Many of these pathotypes are a major public health concern as they have low infectious doses and are transmitted through ubiquitous mediums, including food and water. The seriousness of pathogenic E. coli is exemplified by dedicated national and international surveillance programs that monitor and track outbreaks; unfortunately, this surveillance is often lacking in developing countries. While not all pathotypes carry the same public health profile, they all carry an enormous potential to cause disease and continue to present challenges to human health. This comprehensive review highlights recent advances in our understanding of the intestinal pathotypes of E. coli.

1,097 citations

Journal ArticleDOI
TL;DR: Main approaches to the characterization of proteins and protein complexes using SAXS are reviewed, and main tools for the analysis of proteins in solution are presented, and the impact that these tools have made in modern structural biology is discussed.

517 citations

Journal ArticleDOI
Mary F. Roberts1
TL;DR: The range of solutes, their diverse biosynthetic pathways, and physical properties of the solutes that effect molecular stability are reviewed.
Abstract: Microorganisms that adapt to moderate and high salt environments use a variety of solutes, organic and inorganic, to counter external osmotic pressure. The organic solutes can be zwitterionic, noncharged, or anionic (along with an inorganic cation such as K+). The range of solutes, their diverse biosynthetic pathways, and physical properties of the solutes that effect molecular stability are reviewed.

517 citations