The hetero-hexameric nature of a chloroplast AAA+ FtsH protease contributes to its thermodynamic stability.

FtsH is an evolutionary conserved membrane-bound metalloprotease complex. While in most prokaryotes FtsH is encoded by a single gene, multiple FtsH genes are found in eukaryotes. Genetic and biochemical data suggest that the Arabidopsis chloroplast FtsH is a hetero-hexamer. This raises the question...

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Autores principales:	Ofer Moldavski, Olga Levin-Kravets, Tamar Ziv, Zach Adam, Gali Prag
Formato:	article
Lenguaje:	EN
Publicado:	Public Library of Science (PLoS) 2012
Materias:	Medicine R Science Q
Acceso en línea:	https://doaj.org/article/096ada308a564a9a93d91293d46241b6
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spelling	oai:doaj.org-article:096ada308a564a9a93d91293d46241b62021-11-18T07:20:29ZThe hetero-hexameric nature of a chloroplast AAA+ FtsH protease contributes to its thermodynamic stability.1932-620310.1371/journal.pone.0036008https://doaj.org/article/096ada308a564a9a93d91293d46241b62012-01-01T00:00:00Zhttps://www.ncbi.nlm.nih.gov/pmc/articles/pmid/22558304/pdf/?tool=EBIhttps://doaj.org/toc/1932-6203FtsH is an evolutionary conserved membrane-bound metalloprotease complex. While in most prokaryotes FtsH is encoded by a single gene, multiple FtsH genes are found in eukaryotes. Genetic and biochemical data suggest that the Arabidopsis chloroplast FtsH is a hetero-hexamer. This raises the question why photosynthetic organisms require a heteromeric complex, whereas in most bacteria a homomeric one is sufficient. To gain structural information of the possible complexes, the Arabidopsis FtsH2 (type B) and FtsH5 (type A) were modeled. An in silico study with mixed models of FtsH2/5 suggests that heteromeric hexamer structure with ratio of 4:2 is more likely to exists. Specifically, calculation of the buried surface area at the interfaces between neighboring subunits revealed that a hetero-complex should be thermodynamically more stable than a homo-hexamer, due to the presence of additional hydrophobic and hydrophilic interactions. To biochemically assess this model, we generated Arabidopsis transgenic plants, expressing epitope-tagged FtsH2 and immuno-purified the protein. Mass-spectrometry analysis showed that FtsH2 is associated with FtsH1, FtsH5 and FtsH8. Interestingly, we found that 'type B' subunits (FtsH2 and FtsH8) were 2-3 fold more abundant than 'type A' (FtsH1 and FtsH5). The biochemical data corroborate the in silico model and suggest that the thylakoid FtsH hexamer is composed of two 'type A' and four 'type B' subunits.Ofer MoldavskiOlga Levin-KravetsTamar ZivZach AdamGali PragPublic Library of Science (PLoS)articleMedicineRScienceQENPLoS ONE, Vol 7, Iss 4, p e36008 (2012)
institution	DOAJ
collection	DOAJ
language	EN
topic	Medicine R Science Q
spellingShingle	Medicine R Science Q Ofer Moldavski Olga Levin-Kravets Tamar Ziv Zach Adam Gali Prag The hetero-hexameric nature of a chloroplast AAA+ FtsH protease contributes to its thermodynamic stability.
description	FtsH is an evolutionary conserved membrane-bound metalloprotease complex. While in most prokaryotes FtsH is encoded by a single gene, multiple FtsH genes are found in eukaryotes. Genetic and biochemical data suggest that the Arabidopsis chloroplast FtsH is a hetero-hexamer. This raises the question why photosynthetic organisms require a heteromeric complex, whereas in most bacteria a homomeric one is sufficient. To gain structural information of the possible complexes, the Arabidopsis FtsH2 (type B) and FtsH5 (type A) were modeled. An in silico study with mixed models of FtsH2/5 suggests that heteromeric hexamer structure with ratio of 4:2 is more likely to exists. Specifically, calculation of the buried surface area at the interfaces between neighboring subunits revealed that a hetero-complex should be thermodynamically more stable than a homo-hexamer, due to the presence of additional hydrophobic and hydrophilic interactions. To biochemically assess this model, we generated Arabidopsis transgenic plants, expressing epitope-tagged FtsH2 and immuno-purified the protein. Mass-spectrometry analysis showed that FtsH2 is associated with FtsH1, FtsH5 and FtsH8. Interestingly, we found that 'type B' subunits (FtsH2 and FtsH8) were 2-3 fold more abundant than 'type A' (FtsH1 and FtsH5). The biochemical data corroborate the in silico model and suggest that the thylakoid FtsH hexamer is composed of two 'type A' and four 'type B' subunits.
format	article
author	Ofer Moldavski Olga Levin-Kravets Tamar Ziv Zach Adam Gali Prag
author_facet	Ofer Moldavski Olga Levin-Kravets Tamar Ziv Zach Adam Gali Prag
author_sort	Ofer Moldavski
title	The hetero-hexameric nature of a chloroplast AAA+ FtsH protease contributes to its thermodynamic stability.
title_short	The hetero-hexameric nature of a chloroplast AAA+ FtsH protease contributes to its thermodynamic stability.
title_full	The hetero-hexameric nature of a chloroplast AAA+ FtsH protease contributes to its thermodynamic stability.
title_fullStr	The hetero-hexameric nature of a chloroplast AAA+ FtsH protease contributes to its thermodynamic stability.
title_full_unstemmed	The hetero-hexameric nature of a chloroplast AAA+ FtsH protease contributes to its thermodynamic stability.
title_sort	hetero-hexameric nature of a chloroplast aaa+ ftsh protease contributes to its thermodynamic stability.
publisher	Public Library of Science (PLoS)
publishDate	2012
url	https://doaj.org/article/096ada308a564a9a93d91293d46241b6
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The hetero-hexameric nature of a chloroplast AAA+ FtsH protease contributes to its thermodynamic stability.

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