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Comparative analysis, diversification, and functional validation of plant nucleotide-binding site domain genes.
Hussain, Athar; Khan, Aqsa Anwer; Aslam, Muhammad Qasim; Nazar, Aquib; Zaman, Nadir; Amin, Ayesha; Mahmood, Muhammad Arslan; Mukhtar, M Shahid; Rahman, Hafiz Ubaid Ur; Farooq, Muhammed; Saeed, Muhammed; Amin, Imran; Mansoor, Shahid.
Affiliation
  • Hussain A; National Institute for Biotechnology and Genetic Engineering, College of Pakistan Institute of Engineering and Applied Sciences (PIEAS), Faisalabad, 38000, Pakistan. atharmutahari@gmail.com.
  • Khan AA; School of Food and Agricultural Sciences (SFAS), University of Management and Technology (UMT), Lahore, 54000, Pakistan. atharmutahari@gmail.com.
  • Aslam MQ; Department of Life Science, University of Management and Technology (UMT), Lahore, 54000, Pakistan.
  • Nazar A; National Institute for Biotechnology and Genetic Engineering, College of Pakistan Institute of Engineering and Applied Sciences (PIEAS), Faisalabad, 38000, Pakistan.
  • Zaman N; Department of Life Science, University of Management and Technology (UMT), Lahore, 54000, Pakistan.
  • Amin A; Department of Life Science, University of Management and Technology (UMT), Lahore, 54000, Pakistan.
  • Mahmood MA; Department of Biological Sciences, Superior University, Lahore, 54000, Pakistan.
  • Mukhtar MS; Plant Science Division, Research School of Biology, The Australian National University, Canberra, ACT, 2601, Australia.
  • Rahman HUU; Biosystems Research Complex, Department of Genetics & Biochemistry, Clemson University, Clemson, SC, 29634, USA.
  • Farooq M; School of Food and Agricultural Sciences (SFAS), University of Management and Technology (UMT), Lahore, 54000, Pakistan.
  • Saeed M; National Institute for Biotechnology and Genetic Engineering, College of Pakistan Institute of Engineering and Applied Sciences (PIEAS), Faisalabad, 38000, Pakistan.
  • Amin I; Rheinland-Pfälzische Technische Universität Kaiserslautern-Landau Abteilung Phytopathologie, Paul-Ehrlich-Straße 22, 67653, Kaiserslautern, Germany.
  • Mansoor S; National Institute for Biotechnology and Genetic Engineering, College of Pakistan Institute of Engineering and Applied Sciences (PIEAS), Faisalabad, 38000, Pakistan. imranamin1@yahoo.com.
Sci Rep ; 14(1): 11930, 2024 05 24.
Article in En | MEDLINE | ID: mdl-38789717
ABSTRACT
Nucleotide-binding site (NBS) domain genes are one of the superfamily of resistance genes involved in plant responses to pathogens. The current study identified 12,820 NBS-domain-containing genes across 34 species covering from mosses to monocots and dicots. These identified genes are classified into 168 classes with several novel domain architecture patterns encompassing significant diversity among plant species. Several classical (NBS, NBS-LRR, TIR-NBS, TIR-NBS-LRR, etc.) and species-specific structural patterns (TIR-NBS-TIR-Cupin_1-Cupin_1, TIR-NBS-Prenyltransf, Sugar_tr-NBS etc.) were discovered. We observed 603 orthogroups (OGs) with some core (most common orthogroups; OG0, OG1, OG2, etc.) and unique (highly specific to species; OG80, OG82, etc.) OGs with tandem duplications. The expression profiling presented the putative upregulation of OG2, OG6, and OG15 in different tissues under various biotic and abiotic stresses in susceptible and tolerant plants to cotton leaf curl disease (CLCuD). The genetic variation between susceptible (Coker 312) and tolerant (Mac7) Gossypium hirsutum accessions identified several unique variants in NBS genes of Mac7 (6583 variants) and Coker312 (5173 variants). The protein-ligand and proteins-protein interaction showed a strong interaction of some putative NBS proteins with ADP/ATP and different core proteins of the cotton leaf curl disease virus. The silencing of GaNBS (OG2) in resistant cotton through virus-induced gene silencing (VIGS) demonstrated its putative role in virus tittering. The presented study will be further helpful in understanding the plant adaptation mechanism.
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Full text: 1 Collection: 01-internacional Database: MEDLINE Main subject: Plant Proteins Language: En Journal: Sci Rep Year: 2024 Document type: Article Affiliation country:

Full text: 1 Collection: 01-internacional Database: MEDLINE Main subject: Plant Proteins Language: En Journal: Sci Rep Year: 2024 Document type: Article Affiliation country: