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9. Genome mining of Fusariumreveals structural and functional diversity of pectin lyases: a bioinformatics approach

Author

Yadav, Kanchan, Dwivedi, Shruti, Gupta, Supriya, Dubey, Amit K., Singh, Vinay K., Tanveer, Aiman, Yadav, Sangeeta, and Yadav, Dinesh

Abstract

Pectin lyase (PNL) is an important enzyme of the pectinases group which degrades pectin polymer to 4,5-unsaturated oligogalacturonides by a unique β-elimination mechanism and is used in several industries. The existence of multigene families of pectin lyases has been investigated by mining microbial genomes. In the present study, 52 pectin lyase genes were predicted from sequenced six species of Fusarium,namely F. fujikuroi,F. graminearum,F. proliferatum,F. oxysporum,F. verticillioidesand F. virguliforme.These sequences were in silicocharacterized for several physico-chemical, structural and functional attributes. The translated PNL proteins showed variability with 344–1142 amino acid residues, 35.44–127.41 kDa molecular weight, and pI ranging from 4.63 to 9.28. The aliphatic index ranged from 75.33 to 84.75. Multiple sequence alignment analysis showed several conserved amino acid residues and five distinct groups marked as I, II, III, IV, and V were observed in the phylogenetic tree. The Three-dimensional Structure of five of these PNLs, each representing a distinct group of phylogenetic trees was predicted using I-TASSER Server and validated. The pectin lyase proteins of Fusariumspecies revealed close similarity with pectin lyase of Aspergillus nigerPelA(1IDJ) and PelB(1QCX). Diversity in the structural motifs was observed among Fusariumspecies with 2 β-sheets, 1 β-hairpin, 7–12 β bulges, 18–25 strands, 6 -11 helices, 1 helix-helix interaction, 32–49 β turns, 2–6 γ turns and 2- 3 disulfide bonds. The unique Pec_lyase domain was uniformly observed among all PNL proteins confirming its identity. The genome-wide mining of Fusariumspecies was attempted to provide the diversity of PNLgenes, which could be explored for diverse applications after performing cloning and expression studies.

Published
2022
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10. An FtsH Protease Is Recruited to the Mitochondrion of Plasmodium falciparum.

Author

Tanveer, Aiman, Allen, Stacey M., Jackson, Katherine E., Charan, Manish, Ralph, Stuart A., and Habib, Saman

Subjects
*MITOCHONDRIA, *PLASMODIUM falciparum, *PLASMODIUM, *ANIMAL morphology, *BIOLOGICAL evolution, *MEROZOITES, *ADENOSINE triphosphate, *MEMBRANE proteins
Abstract

The two organelles, apicoplast and mitochondrion, of the malaria parasite Plasmodium falciparum have unique morphology in liver and blood stages; they undergo complex branching and looping prior to division and segregation into daughter merozoites. Little is known about the molecular processes and proteins involved in organelle biogenesis in the parasite. We report the identification of an AAA+/FtsH protease homolog (PfFtsH1) that exhibits ATP- and Zn2+-dependent protease activity. PfFtsH1 undergoes processing, forms oligomeric assemblies, and is associated with the membrane fraction of the parasite cell. Generation of a transfectant parasite line with hemagglutinin-tagged PfFtsH1, and immunofluorescence assay with anti-PfFtsH1 Ab demonstrated that the protein localises to P. falciparum mitochondria. Phylogenetic analysis and the single transmembrane region identifiable in PfFtsH1 suggest that it is an i-AAA like inner mitochondrial membrane protein. Expression of PfFtsH1 in Escherichia coli converted a fraction of bacterial cells into division-defective filamentous forms implying a sequestering effect of the Plasmodium factor on the bacterial homolog, indicative of functional conservation with EcFtsH. These results identify a membrane-associated mitochondrial AAA+/FtsH protease as a candidate regulatory protein for organelle biogenesis in P. falciparum. [ABSTRACT FROM AUTHOR]

Published
2013
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11. An FtsH Protease Is Recruited to the Mitochondrion of Plasmodium falciparum.

Author

Tanveer, Aiman, Allen, Stacey M., Jackson, Katherine E., Charan, Manish, Ralph, Stuart A., and Habib, Saman

Subjects
MITOCHONDRIA, PLASMODIUM falciparum, PLASMODIUM, ANIMAL morphology, BIOLOGICAL evolution, MEROZOITES, ADENOSINE triphosphate, MEMBRANE proteins
Abstract

The two organelles, apicoplast and mitochondrion, of the malaria parasite Plasmodium falciparum have unique morphology in liver and blood stages; they undergo complex branching and looping prior to division and segregation into daughter merozoites. Little is known about the molecular processes and proteins involved in organelle biogenesis in the parasite. We report the identification of an AAA+/FtsH protease homolog (PfFtsH1) that exhibits ATP- and Zn2+-dependent protease activity. PfFtsH1 undergoes processing, forms oligomeric assemblies, and is associated with the membrane fraction of the parasite cell. Generation of a transfectant parasite line with hemagglutinin-tagged PfFtsH1, and immunofluorescence assay with anti-PfFtsH1 Ab demonstrated that the protein localises to P. falciparum mitochondria. Phylogenetic analysis and the single transmembrane region identifiable in PfFtsH1 suggest that it is an i-AAA like inner mitochondrial membrane protein. Expression of PfFtsH1 in Escherichia coli converted a fraction of bacterial cells into division-defective filamentous forms implying a sequestering effect of the Plasmodium factor on the bacterial homolog, indicative of functional conservation with EcFtsH. These results identify a membrane-associated mitochondrial AAA+/FtsH protease as a candidate regulatory protein for organelle biogenesis in P. falciparum. [ABSTRACT FROM AUTHOR]

Published
2013
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