Diversity and Regulation of S-Adenosylmethionine Dependent Methyltransferases in the Anhydrobiotic Midge
Multiple co-localized paralogs of genes in <i>Polypedilum vanderplanki’s</i> genome have strong transcriptional response to dehydration and considered to be a part of adaptation machinery at the larvae stage. One group of such genes represented by L-isoaspartate O-methyltransferases (PIM...
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doaj-06741cdc44214a798a5246d4756807992020-11-25T03:28:48ZengMDPI AGInsects2075-44502020-09-011163463410.3390/insects11090634Diversity and Regulation of S-Adenosylmethionine Dependent Methyltransferases in the Anhydrobiotic MidgeRuslan Deviatiiarov0Rustam Ayupov1Alexander Laikov2Elena Shagimardanova3Takahiro Kikawada4Oleg Gusev5Institute of Fundamental Medicine and Biology, Kazan Federal University, Kazan, Tatarstan 420008, RussiaDepartment of Cell Biology, SUNY Downstate Health Sciences University, Brooklyn, NY 11203, USAInstitute of Fundamental Medicine and Biology, Kazan Federal University, Kazan, Tatarstan 420008, RussiaInstitute of Fundamental Medicine and Biology, Kazan Federal University, Kazan, Tatarstan 420008, RussiaAnhydrobiosis Research Group, Molecular Biomimetics Research Unit, Institute of Agrobiological Sciences, National Institute of Agriculture and Food Research Organization (NARO), Tsukuba 305-0851, JapanInstitute of Fundamental Medicine and Biology, Kazan Federal University, Kazan, Tatarstan 420008, RussiaMultiple co-localized paralogs of genes in <i>Polypedilum vanderplanki’s</i> genome have strong transcriptional response to dehydration and considered to be a part of adaptation machinery at the larvae stage. One group of such genes represented by L-isoaspartate O-methyltransferases (PIMT). In order to highlight specific role of PIMT paralogization in desiccation tolerance of the larvae we annotated and compared S-adenosylmethionine (SAM) dependent methyltransferases of four insect species. From another side we applied co-expression analysis in desiccation/rehydration time course and showed that PIMT coding genes could be separated into five clusters by expression profile. We found that among <i>Polypedilum vanderplanki’s</i> PIMTs only PIMT1 and PIMT2 have enzymatic activity in normal physiological conditions. From in silico analysis of the protein structures we found two highly variable regions outside of the active center, but also amino acid substitutions which may affect SAM stabilization. Overall, in this study we demonstrated features of <i>Polypedilum vanderplanki’s</i> PIMT coding paralogs related to different roles in desiccation tolerance of the larvae. Our results also suggest a role of different SAM-methyltransferases in the adaptation, including GSMT, JHAMT, and candidates from other classes, which could be considered in future studies.https://www.mdpi.com/2075-4450/11/9/634SAM-dependent methyltransferasesPIMT<i>Polypedilum vanderplanki</i>anhydrobiosistranscriptomics |
collection |
DOAJ |
language |
English |
format |
Article |
sources |
DOAJ |
author |
Ruslan Deviatiiarov Rustam Ayupov Alexander Laikov Elena Shagimardanova Takahiro Kikawada Oleg Gusev |
spellingShingle |
Ruslan Deviatiiarov Rustam Ayupov Alexander Laikov Elena Shagimardanova Takahiro Kikawada Oleg Gusev Diversity and Regulation of S-Adenosylmethionine Dependent Methyltransferases in the Anhydrobiotic Midge Insects SAM-dependent methyltransferases PIMT <i>Polypedilum vanderplanki</i> anhydrobiosis transcriptomics |
author_facet |
Ruslan Deviatiiarov Rustam Ayupov Alexander Laikov Elena Shagimardanova Takahiro Kikawada Oleg Gusev |
author_sort |
Ruslan Deviatiiarov |
title |
Diversity and Regulation of S-Adenosylmethionine Dependent Methyltransferases in the Anhydrobiotic Midge |
title_short |
Diversity and Regulation of S-Adenosylmethionine Dependent Methyltransferases in the Anhydrobiotic Midge |
title_full |
Diversity and Regulation of S-Adenosylmethionine Dependent Methyltransferases in the Anhydrobiotic Midge |
title_fullStr |
Diversity and Regulation of S-Adenosylmethionine Dependent Methyltransferases in the Anhydrobiotic Midge |
title_full_unstemmed |
Diversity and Regulation of S-Adenosylmethionine Dependent Methyltransferases in the Anhydrobiotic Midge |
title_sort |
diversity and regulation of s-adenosylmethionine dependent methyltransferases in the anhydrobiotic midge |
publisher |
MDPI AG |
series |
Insects |
issn |
2075-4450 |
publishDate |
2020-09-01 |
description |
Multiple co-localized paralogs of genes in <i>Polypedilum vanderplanki’s</i> genome have strong transcriptional response to dehydration and considered to be a part of adaptation machinery at the larvae stage. One group of such genes represented by L-isoaspartate O-methyltransferases (PIMT). In order to highlight specific role of PIMT paralogization in desiccation tolerance of the larvae we annotated and compared S-adenosylmethionine (SAM) dependent methyltransferases of four insect species. From another side we applied co-expression analysis in desiccation/rehydration time course and showed that PIMT coding genes could be separated into five clusters by expression profile. We found that among <i>Polypedilum vanderplanki’s</i> PIMTs only PIMT1 and PIMT2 have enzymatic activity in normal physiological conditions. From in silico analysis of the protein structures we found two highly variable regions outside of the active center, but also amino acid substitutions which may affect SAM stabilization. Overall, in this study we demonstrated features of <i>Polypedilum vanderplanki’s</i> PIMT coding paralogs related to different roles in desiccation tolerance of the larvae. Our results also suggest a role of different SAM-methyltransferases in the adaptation, including GSMT, JHAMT, and candidates from other classes, which could be considered in future studies. |
topic |
SAM-dependent methyltransferases PIMT <i>Polypedilum vanderplanki</i> anhydrobiosis transcriptomics |
url |
https://www.mdpi.com/2075-4450/11/9/634 |
work_keys_str_mv |
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