New group of transmembrane proteins associated with desiccation tolerance in the anhydrobiotic midge Polypedilum vanderplanki

Abstract Larvae of the sleeping chironomid Polypedilum vanderplanki are known for their extraordinary ability to survive complete desiccation in an ametabolic state called “anhydrobiosis”. The unique feature of P. vanderplanki genome is the presence of expanded gene clusters associated with anhydrob...

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Autores principales:	Taisiya A. Voronina, Alexander A. Nesmelov, Sabina A. Kondratyeva, Ruslan M. Deviatiiarov, Yugo Miyata, Shoko Tokumoto, Richard Cornette, Oleg A. Gusev, Takahiro Kikawada, Elena I. Shagimardanova
Formato:	article
Lenguaje:	EN
Publicado:	Nature Portfolio 2020
Materias:	Medicine R Science Q
Acceso en línea:	https://doaj.org/article/c79d9291961944d7ad61a17de592df2e
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spelling	oai:doaj.org-article:c79d9291961944d7ad61a17de592df2e2021-12-02T15:32:59ZNew group of transmembrane proteins associated with desiccation tolerance in the anhydrobiotic midge Polypedilum vanderplanki10.1038/s41598-020-68330-62045-2322https://doaj.org/article/c79d9291961944d7ad61a17de592df2e2020-07-01T00:00:00Zhttps://doi.org/10.1038/s41598-020-68330-6https://doaj.org/toc/2045-2322Abstract Larvae of the sleeping chironomid Polypedilum vanderplanki are known for their extraordinary ability to survive complete desiccation in an ametabolic state called “anhydrobiosis”. The unique feature of P. vanderplanki genome is the presence of expanded gene clusters associated with anhydrobiosis. While several such clusters represent orthologues of known genes, there is a distinct set of genes unique for P. vanderplanki. These include Lea-Island-Located (LIL) genes with no known orthologues except two of LEA genes of P. vanderplanki, PvLea1 and PvLea3. However, PvLIL proteins lack typical features of LEA such as the state of intrinsic disorder, hydrophilicity and characteristic LEA_4 motif. They possess four to five transmembrane domains each and we confirmed membrane targeting for three PvLILs. Conserved amino acids in PvLIL are located in transmembrane domains or nearby. PvLEA1 and PvLEA3 proteins are chimeras combining LEA-like parts and transmembrane domains, shared with PvLIL proteins. We have found that PvLil genes are highly upregulated during anhydrobiosis induction both in larvae of P. vanderplanki and P. vanderplanki-derived cultured cell line, Pv11. Thus, PvLil are a new intriguing group of genes that are likely to be associated with anhydrobiosis due to their common origin with some LEA genes and their induction during anhydrobiosis.Taisiya A. VoroninaAlexander A. NesmelovSabina A. KondratyevaRuslan M. DeviatiiarovYugo MiyataShoko TokumotoRichard CornetteOleg A. GusevTakahiro KikawadaElena I. ShagimardanovaNature PortfolioarticleMedicineRScienceQENScientific Reports, Vol 10, Iss 1, Pp 1-13 (2020)
institution	DOAJ
collection	DOAJ
language	EN
topic	Medicine R Science Q
spellingShingle	Medicine R Science Q Taisiya A. Voronina Alexander A. Nesmelov Sabina A. Kondratyeva Ruslan M. Deviatiiarov Yugo Miyata Shoko Tokumoto Richard Cornette Oleg A. Gusev Takahiro Kikawada Elena I. Shagimardanova New group of transmembrane proteins associated with desiccation tolerance in the anhydrobiotic midge Polypedilum vanderplanki
description	Abstract Larvae of the sleeping chironomid Polypedilum vanderplanki are known for their extraordinary ability to survive complete desiccation in an ametabolic state called “anhydrobiosis”. The unique feature of P. vanderplanki genome is the presence of expanded gene clusters associated with anhydrobiosis. While several such clusters represent orthologues of known genes, there is a distinct set of genes unique for P. vanderplanki. These include Lea-Island-Located (LIL) genes with no known orthologues except two of LEA genes of P. vanderplanki, PvLea1 and PvLea3. However, PvLIL proteins lack typical features of LEA such as the state of intrinsic disorder, hydrophilicity and characteristic LEA_4 motif. They possess four to five transmembrane domains each and we confirmed membrane targeting for three PvLILs. Conserved amino acids in PvLIL are located in transmembrane domains or nearby. PvLEA1 and PvLEA3 proteins are chimeras combining LEA-like parts and transmembrane domains, shared with PvLIL proteins. We have found that PvLil genes are highly upregulated during anhydrobiosis induction both in larvae of P. vanderplanki and P. vanderplanki-derived cultured cell line, Pv11. Thus, PvLil are a new intriguing group of genes that are likely to be associated with anhydrobiosis due to their common origin with some LEA genes and their induction during anhydrobiosis.
format	article
author	Taisiya A. Voronina Alexander A. Nesmelov Sabina A. Kondratyeva Ruslan M. Deviatiiarov Yugo Miyata Shoko Tokumoto Richard Cornette Oleg A. Gusev Takahiro Kikawada Elena I. Shagimardanova
author_facet	Taisiya A. Voronina Alexander A. Nesmelov Sabina A. Kondratyeva Ruslan M. Deviatiiarov Yugo Miyata Shoko Tokumoto Richard Cornette Oleg A. Gusev Takahiro Kikawada Elena I. Shagimardanova
author_sort	Taisiya A. Voronina
title	New group of transmembrane proteins associated with desiccation tolerance in the anhydrobiotic midge Polypedilum vanderplanki
title_short	New group of transmembrane proteins associated with desiccation tolerance in the anhydrobiotic midge Polypedilum vanderplanki
title_full	New group of transmembrane proteins associated with desiccation tolerance in the anhydrobiotic midge Polypedilum vanderplanki
title_fullStr	New group of transmembrane proteins associated with desiccation tolerance in the anhydrobiotic midge Polypedilum vanderplanki
title_full_unstemmed	New group of transmembrane proteins associated with desiccation tolerance in the anhydrobiotic midge Polypedilum vanderplanki
title_sort	new group of transmembrane proteins associated with desiccation tolerance in the anhydrobiotic midge polypedilum vanderplanki
publisher	Nature Portfolio
publishDate	2020
url	https://doaj.org/article/c79d9291961944d7ad61a17de592df2e
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New group of transmembrane proteins associated with desiccation tolerance in the anhydrobiotic midge Polypedilum vanderplanki

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