Mrinal K. Maiti

Indian Institute of Technology Kharagpur

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Soumitra K. Sen

Indian Institute of Technology Kharagpur

Asitava Basu

Indian Institute of Technology Kharagpur

Atrayee Chattopadhyay

Long Island University

Natasha Das

Indian Institute of Technology Kharagpur

Prabuddha Dey

Rutgers, The State University of New Jersey

Surajit Bhattacharya

Sahara Hospital

Adinpunya Mitra

Indian Institute of Technology Kharagpur

Srimonta Gayen

Indian Institute of Science Bangalore

Amit Kumar Das

Indian Institute of Technology Kharagpur

Joydeep Banerjee

Indian Institute of Technology Kharagpur

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Indian Institute of Technology Kharagpur

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GSI Helmholtz Centre for Heavy Ion Research

Indian Institute of Technology Indore

Johannes Gutenberg University Mainz

Helmholtz Institute Mainz

Bose Institute

Lund University

Lawrence Berkeley National Laboratory

University of California, Berkeley

Bidhan Chandra Krishi Viswavidyalaya

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Characterization and cloning of a stearoyl/oleoyl specific fatty acyl-acyl carrier protein thioesterase from the seeds of Madhuca longifolia (latifolia)

Plant Physiology and Biochemistry (2007)

Santosh K. Ghosh Ashis Bhattacharjee Jyoti K. Jha Ashis K. Mondal Mrinal K. Maiti

Thioesterase

Stearate

10.1016/j.plaphy.2007.09.003

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Citations (25)

Knockout of fatty acid elongase1 homeoalleles in amphidiploid Brassica juncea leads to undetectable erucic acid in seed oil

bioRxiv (Cold Spring Harbor Laboratory) (2024)

Neelesh Patra Guy C. Barker Mrinal K. Maiti

Summary Indian mustard ( Brassica juncea L.) is a major oilseed crop with significant economic and nutritional importance within the Indian subcontinent. While its seed oil offers valuable dietary benefits, including a balanced ratio of human essential fatty acids, the traditional high oil-yielding varieties contain an elevated level of erucic acid (EA, C22:1) that is associated with adverse health effects. Therefore, developing low erucic acid (LEA) mustard cultivars is crucial for broader utilization and consumer safety. In this study, we employed CRISPR/Cas9 genome editing tools to disrupt the fatty acid elongase1 ( FAE1 ) gene that encodes a key enzyme in EA biosynthesis in two high erucic acid (HEA) B. juncea cultivars, PCR7 and JD6. Targeted knockout (KO) of BjFAE1 homeoalleles ( BjFAE1.1 and BjFAE1.2 ) in this amphidiploid plant using CRISPR/Cas9 constructs, each carrying two guide RNAs led to monoallelic and biallelic mutations. Biallelic KO lines showed a near-complete elimination of EA (<0.5% in PCR7, undetectable in JD6) with a significant increase in nutritionally beneficial oleic acid (∼30% in PCR7, ∼35% in JD6), while the content of essential fatty acids also increased significantly, suggesting rerouting of carbon flux from EA biosynthesis. Importantly, these LEA lines retained key agronomic traits like plant seed yield and oil content, matching the productivity of the control elite cultivars. Our findings underscore the effectiveness of CRISPR/Cas9 technology for editing B. juncea genome, producing LEA seed oil lines with improved nutritional quality and thus expanding the applications of this important oilseed crop.

Erucic acid

10.1101/2024.10.09.617390

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Acyl carrier protein of Azospirillum brasilense: properties of the purified protein and sequencing of the corresponding gene, acpP

Microbiology (1996)

Mrinal K. Maiti Sudipta Ghosh

Acyl carrier protein (ACP) plays a crucial role in bacterial fatty acid synthesis. Cloning genes encoding ACPs from Gram-negative bacteria in Escherichia coli is difficult due to adverse effects of the cloned gene on host cell viability, and we were unsuccessful in cloning the full length ACP gene (acpP) from Azospirillum brasilense using conventional methods. Therefore, ACP from A. brasilense was purified to homogeneity and a part of the acpP gene was cloned using the polymerase chain reaction (PCR) technique with two primers, one designed from the N-terminal amino acid sequence of the purified ACP and the other from the highly conserved amino acid sequence of bacterial ACPs. The nucleotide sequence of the gene was obtained by cloning and sequencing inverse PCR products containing the acpP region generated by two oppositely oriented internal primers designed from the partial acpP gene sequence using restriction-enzyme-digested, self-circularized chromosomal DNA fragments as templates. Characterization of the purified ACP and analysis of the derived amino acid sequence of the acpP gene of A. brasilense revealed that: (a) the mature ACP, composed of 78 amino acids, is a highly expressed protein (about 2·0–3·0 × 104 molecules per cell), (b) compared to E. coli ACP, it has a more compact structure and contains significantly more hydrophobic amino acid residues and (c) the potential mRNA sequence of the ACP gene has some structural features typical of a stable mRNA.

Azospirillum brasilense

10.1099/13500872-142-8-2097

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Differential effect of elevated carbon dioxide on sucrose transport and accumulation in developing grains of three rice cultivars

Plant Gene (2021)

Usha Rani Jena Surajit Bhattacharya Dillip Kumar Swain Mrinal K. Maiti

Differential effects

10.1016/j.plgene.2021.100337

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The attack of the phytopathogens and the trumpet solo: Identification of a novel plant antifungal peptide with distinct fold and disulfide bond pattern

Biochimie (2013)

Santi M. Mandal William F. Porto Prabuddha Dey Mrinal K. Maiti Ananta K. Ghosh

Phytopathogens cause economic losses in agribusiness. Plant-derived compounds have been proposed to overcome this problem, including the antimicrobial peptides (AMPs). This paper reports the identification of Ps-AFP1, a novel AMP isolated from the Pisum sativum radicle. Ps-AFP1 was purified and evaluated against phytopathogenic fungi, showing clear effectiveness. In silico analyses were performed, suggesting an unusual fold and disulfide bond pattern. A novel fold and a novel AMP class were here proposed, the αβ-trumpet fold and αβ-trumpet peptides, respectively. The name αβ-trumpet was created due to the peptide's fold, which resembles the musical instrument. The Ps-AFP1 mechanism of action was also proposed. Microscopic analyses revealed that Ps-AFP1 could affect the fungus during the hyphal elongation from spore germination. Furthermore, confocal microscopy performed with Ps-AFP1 labeled with FITC shows that the peptide was localized at high concentration along the fungal cell surface. Due to low cellular disruption rates, it seems that the main target is the fungal cell wall. The binding thermogram and isothermal titration, molecular dynamics and docking analyses were also performed, showing that Ps-AFP1 could bind to chitin producing a stable complex. Data here reported provided novel structural–functional insights into the αβ-trumpet peptide fold.

10.1016/j.biochi.2013.06.027

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Citations (28)

Molecular characterization of glyoxalase II from Arabidopsis thaliana.

Plant Molecular Biology (1997)

Mrinal K. Maiti S. Krishnasamy Heather Owen Christopher A. Makaroff

Lactoylglutathione lyase

10.1023/a:1005891123344

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Citations (80)

Fruity-scented antifungal volatiles from endophytic Geotrichum candidum PF005: Broad-spectrum bioactivity against stored grain pathogens, mode of action and suitable formulation for mycofumigation

Biological Control (2022)