HcRed, a genetically encoded fluorescent binary cross-linking agent for cross-linking of mitochondrial ATP synthase in Saccharomyces cerevisiae.

Genetically encoded fluorescent cross-linking agents represent powerful tools useful both for visualising and modulating protein interactions in living cells. The far-red fluorescent protein HcRed, which is fluorescent only in a dimer form, can be used to promote the homo-dimerisation of target prot...

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Autores principales:	Lan Gong, Georg Ramm, Rodney J Devenish, Mark Prescott
Formato:	article
Lenguaje:	EN
Publicado:	Public Library of Science (PLoS) 2012
Materias:	Medicine R Science Q
Acceso en línea:	https://doaj.org/article/e1ad394ce6c1470ba986492809f182de
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spelling	oai:doaj.org-article:e1ad394ce6c1470ba986492809f182de2021-11-18T07:23:09ZHcRed, a genetically encoded fluorescent binary cross-linking agent for cross-linking of mitochondrial ATP synthase in Saccharomyces cerevisiae.1932-620310.1371/journal.pone.0035095https://doaj.org/article/e1ad394ce6c1470ba986492809f182de2012-01-01T00:00:00Zhttps://www.ncbi.nlm.nih.gov/pmc/articles/pmid/22496895/?tool=EBIhttps://doaj.org/toc/1932-6203Genetically encoded fluorescent cross-linking agents represent powerful tools useful both for visualising and modulating protein interactions in living cells. The far-red fluorescent protein HcRed, which is fluorescent only in a dimer form, can be used to promote the homo-dimerisation of target proteins, and thereby yield useful information about biological processes. We have in yeast cells expressed HcRed fused to a subunit of mitochondrial ATP synthase (mtATPase). This resulted in cross-linking of the large multi-subunit mtATPase complex within the inner-membrane of the mitochondrion. Fluorescence microscopy revealed aberrant mitochondrial morphology, and mtATPase complexes isolated from mitochondria were recovered as fluorescent dimers under conditions where complexes from control mitochondria were recovered as monomers. When viewed by electron microscopy normal cristae were absent from mitochondria in cells in which mATPase complexes were cross-linked. mtATPase dimers are believed to be the building blocks that are assembled into supramolecular mtATPase ribbons that promote the formation of mitochondrial cristae. We propose that HcRed cross-links mATPase complexes in the mitochondrial membrane hindering the normal assembly/disassembly of the supramolecular forms of mtATPase.Lan GongGeorg RammRodney J DevenishMark PrescottPublic Library of Science (PLoS)articleMedicineRScienceQENPLoS ONE, Vol 7, Iss 4, p e35095 (2012)
institution	DOAJ
collection	DOAJ
language	EN
topic	Medicine R Science Q
spellingShingle	Medicine R Science Q Lan Gong Georg Ramm Rodney J Devenish Mark Prescott HcRed, a genetically encoded fluorescent binary cross-linking agent for cross-linking of mitochondrial ATP synthase in Saccharomyces cerevisiae.
description	Genetically encoded fluorescent cross-linking agents represent powerful tools useful both for visualising and modulating protein interactions in living cells. The far-red fluorescent protein HcRed, which is fluorescent only in a dimer form, can be used to promote the homo-dimerisation of target proteins, and thereby yield useful information about biological processes. We have in yeast cells expressed HcRed fused to a subunit of mitochondrial ATP synthase (mtATPase). This resulted in cross-linking of the large multi-subunit mtATPase complex within the inner-membrane of the mitochondrion. Fluorescence microscopy revealed aberrant mitochondrial morphology, and mtATPase complexes isolated from mitochondria were recovered as fluorescent dimers under conditions where complexes from control mitochondria were recovered as monomers. When viewed by electron microscopy normal cristae were absent from mitochondria in cells in which mATPase complexes were cross-linked. mtATPase dimers are believed to be the building blocks that are assembled into supramolecular mtATPase ribbons that promote the formation of mitochondrial cristae. We propose that HcRed cross-links mATPase complexes in the mitochondrial membrane hindering the normal assembly/disassembly of the supramolecular forms of mtATPase.
format	article
author	Lan Gong Georg Ramm Rodney J Devenish Mark Prescott
author_facet	Lan Gong Georg Ramm Rodney J Devenish Mark Prescott
author_sort	Lan Gong
title	HcRed, a genetically encoded fluorescent binary cross-linking agent for cross-linking of mitochondrial ATP synthase in Saccharomyces cerevisiae.
title_short	HcRed, a genetically encoded fluorescent binary cross-linking agent for cross-linking of mitochondrial ATP synthase in Saccharomyces cerevisiae.
title_full	HcRed, a genetically encoded fluorescent binary cross-linking agent for cross-linking of mitochondrial ATP synthase in Saccharomyces cerevisiae.
title_fullStr	HcRed, a genetically encoded fluorescent binary cross-linking agent for cross-linking of mitochondrial ATP synthase in Saccharomyces cerevisiae.
title_full_unstemmed	HcRed, a genetically encoded fluorescent binary cross-linking agent for cross-linking of mitochondrial ATP synthase in Saccharomyces cerevisiae.
title_sort	hcred, a genetically encoded fluorescent binary cross-linking agent for cross-linking of mitochondrial atp synthase in saccharomyces cerevisiae.
publisher	Public Library of Science (PLoS)
publishDate	2012
url	https://doaj.org/article/e1ad394ce6c1470ba986492809f182de
work_keys_str_mv	AT langong hcredageneticallyencodedfluorescentbinarycrosslinkingagentforcrosslinkingofmitochondrialatpsynthaseinsaccharomycescerevisiae AT georgramm hcredageneticallyencodedfluorescentbinarycrosslinkingagentforcrosslinkingofmitochondrialatpsynthaseinsaccharomycescerevisiae AT rodneyjdevenish hcredageneticallyencodedfluorescentbinarycrosslinkingagentforcrosslinkingofmitochondrialatpsynthaseinsaccharomycescerevisiae AT markprescott hcredageneticallyencodedfluorescentbinarycrosslinkingagentforcrosslinkingofmitochondrialatpsynthaseinsaccharomycescerevisiae
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HcRed, a genetically encoded fluorescent binary cross-linking agent for cross-linking of mitochondrial ATP synthase in Saccharomyces cerevisiae.

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