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Study of subcellular localization of Glycine max ?-tocopherol methyl transferase isoforms in N. benthamiana.

ABSTRACT: Gamma-tocopherol methyltransferase (?-TMT) converts ?-toc to ?-toc-the rate limiting step in toc biosynthesis. Sequencing results revealed that the coding regions of ?-TMT1 and ?-TMT3 were strongly similar to each other (93% at amino acid level). Based on the differences in the N-terminal amino acids, Glycine max-?-TMT proteins are categorized into three isoforms: ?-TMT1, 2 and 3. In silico structural analysis revealed the presence of chloroplast transit peptide (cTP) in ?-TMT1 and ?-TMT3 protein. However, other properties of transit peptide like presence of hydrophobic amino acids at the first three positions of N-terminal end and lower level of acidic amino acids were revealed only in ?-TMT3 protein. Subcellular localization of GFP fused ?-TMT1 and ?-TMT3 under 35S promoter was studied in Nicotiana benthamiana using confocal microscopy. Results showed that ?-TMT1 was found in the cytosol and ?-TMT3 was found to be localized both in cytosol and chloroplast. Further the presence ?-TMT3 in chloroplast was validated by quantifying ?-tocopherol through UPLC. Thus the present study of cytosolic localization of the both ?-TMT1 and ?-TMT3 proteins and chloroplastic localization of ?-TMT3 will help to reveal the importance of ?-TMT encoded ?-toc in protecting both chloroplastic and cell membrane from plant oxidative stress.

SUBMITTER: Kumari K 

PROVIDER: S-EPMC7013018 | biostudies-literature | 2020 Mar

REPOSITORIES: biostudies-literature

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Study of subcellular localization of <i>Glycine max</i> γ-tocopherol methyl transferase isoforms in <i>N. benthamiana</i>.

Kumari Khushboo K   Rai Monika Prakash MP   Bansal Navita N   Prashat G Rama GR   Kumari Sweta S   Srivathsa Rohini R   Dahuja Anil A   Sachdev Archana A   Praveen Shelly S   Vinutha T T  

3 Biotech 20200211 3

Gamma-tocopherol methyltransferase (γ-TMT) converts γ-toc to α-toc-the rate limiting step in toc biosynthesis. Sequencing results revealed that the coding regions of <i>γ-TMT1</i> and <i>γ-TMT3</i> were strongly similar to each other (93% at amino acid level). Based on the differences in the N-terminal amino acids, <i>Glycine max</i>-<i>γ</i>-TMT proteins are categorized into three isoforms: γ-TMT1, 2 and 3. In silico structural analysis revealed the presence of chloroplast transit peptide (cTP)  ...[more]

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