Reduction in structural disorder and functional complexity in the thermal adaptation of prokaryotes.

Genomic correlates of evolutionary adaptation to very low or very high optimal growth temperature (OGT) values have been the subject of many studies. Whereas these provided a protein-structural rationale of the activity and stability of globular proteins/enzymes, the point has been neglected that ad...

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Autores principales:	Prasad V Burra, Lajos Kalmar, Peter Tompa
Formato:	article
Lenguaje:	EN
Publicado:	Public Library of Science (PLoS) 2010
Materias:	Medicine R Science Q
Acceso en línea:	https://doaj.org/article/785dacb1976a444591dfd5841df80371
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spelling	oai:doaj.org-article:785dacb1976a444591dfd5841df803712021-11-18T06:36:10ZReduction in structural disorder and functional complexity in the thermal adaptation of prokaryotes.1932-620310.1371/journal.pone.0012069https://doaj.org/article/785dacb1976a444591dfd5841df803712010-08-01T00:00:00Zhttps://www.ncbi.nlm.nih.gov/pmc/articles/pmid/20711457/pdf/?tool=EBIhttps://doaj.org/toc/1932-6203Genomic correlates of evolutionary adaptation to very low or very high optimal growth temperature (OGT) values have been the subject of many studies. Whereas these provided a protein-structural rationale of the activity and stability of globular proteins/enzymes, the point has been neglected that adaptation to extreme temperatures could also have resulted from an increased use of intrinsically disordered proteins (IDPs), which are resistant to these conditions in vitro. Contrary to these expectations, we found a conspicuously low level of structural disorder in bacteria of very high (and very low) OGT values. This paucity of disorder does not reflect phylogenetic relatedness, i.e. it is a result of genuine adaptation to extreme conditions. Because intrinsic disorder correlates with important regulatory functions, we asked how these bacteria could exist without IDPs by studying transcription factors, known to harbor a lot of function-related intrinsic disorder. Hyperthermophiles have much less transcription factors, which have reduced disorder compared to their mesophilic counterparts. On the other hand, we found by systematic categorization of proteins with long disordered regions that there are certain functions, such as translation and ribosome biogenesis that depend on structural disorder even in hyperthermophiles. In all, our observations suggest that adaptation to extreme conditions is achieved by a significant functional simplification, apparent at both the level of the genome and individual genes/proteins.Prasad V BurraLajos KalmarPeter TompaPublic Library of Science (PLoS)articleMedicineRScienceQENPLoS ONE, Vol 5, Iss 8, p e12069 (2010)
institution	DOAJ
collection	DOAJ
language	EN
topic	Medicine R Science Q
spellingShingle	Medicine R Science Q Prasad V Burra Lajos Kalmar Peter Tompa Reduction in structural disorder and functional complexity in the thermal adaptation of prokaryotes.
description	Genomic correlates of evolutionary adaptation to very low or very high optimal growth temperature (OGT) values have been the subject of many studies. Whereas these provided a protein-structural rationale of the activity and stability of globular proteins/enzymes, the point has been neglected that adaptation to extreme temperatures could also have resulted from an increased use of intrinsically disordered proteins (IDPs), which are resistant to these conditions in vitro. Contrary to these expectations, we found a conspicuously low level of structural disorder in bacteria of very high (and very low) OGT values. This paucity of disorder does not reflect phylogenetic relatedness, i.e. it is a result of genuine adaptation to extreme conditions. Because intrinsic disorder correlates with important regulatory functions, we asked how these bacteria could exist without IDPs by studying transcription factors, known to harbor a lot of function-related intrinsic disorder. Hyperthermophiles have much less transcription factors, which have reduced disorder compared to their mesophilic counterparts. On the other hand, we found by systematic categorization of proteins with long disordered regions that there are certain functions, such as translation and ribosome biogenesis that depend on structural disorder even in hyperthermophiles. In all, our observations suggest that adaptation to extreme conditions is achieved by a significant functional simplification, apparent at both the level of the genome and individual genes/proteins.
format	article
author	Prasad V Burra Lajos Kalmar Peter Tompa
author_facet	Prasad V Burra Lajos Kalmar Peter Tompa
author_sort	Prasad V Burra
title	Reduction in structural disorder and functional complexity in the thermal adaptation of prokaryotes.
title_short	Reduction in structural disorder and functional complexity in the thermal adaptation of prokaryotes.
title_full	Reduction in structural disorder and functional complexity in the thermal adaptation of prokaryotes.
title_fullStr	Reduction in structural disorder and functional complexity in the thermal adaptation of prokaryotes.
title_full_unstemmed	Reduction in structural disorder and functional complexity in the thermal adaptation of prokaryotes.
title_sort	reduction in structural disorder and functional complexity in the thermal adaptation of prokaryotes.
publisher	Public Library of Science (PLoS)
publishDate	2010
url	https://doaj.org/article/785dacb1976a444591dfd5841df80371
work_keys_str_mv	AT prasadvburra reductioninstructuraldisorderandfunctionalcomplexityinthethermaladaptationofprokaryotes AT lajoskalmar reductioninstructuraldisorderandfunctionalcomplexityinthethermaladaptationofprokaryotes AT petertompa reductioninstructuraldisorderandfunctionalcomplexityinthethermaladaptationofprokaryotes
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Reduction in structural disorder and functional complexity in the thermal adaptation of prokaryotes.

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