Cargando…
PucC and LhaA direct efficient assembly of the light‐harvesting complexes in Rhodobacter sphaeroides
The mature architecture of the photosynthetic membrane of the purple phototroph R hodobacter sphaeroides has been characterised to a level where an atomic‐level membrane model is available, but the roles of the putative assembly proteins LhaA and PucC in establishing this architecture are unknown. H...
Autores principales: | , , , , , , |
---|---|
Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
John Wiley and Sons Inc.
2015
|
Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4949548/ https://www.ncbi.nlm.nih.gov/pubmed/26419219 http://dx.doi.org/10.1111/mmi.13235 |
_version_ | 1782443449783418880 |
---|---|
author | Mothersole, David J. Jackson, Philip J. Vasilev, Cvetelin Tucker, Jaimey D. Brindley, Amanda A. Dickman, Mark J. Hunter, C. Neil |
author_facet | Mothersole, David J. Jackson, Philip J. Vasilev, Cvetelin Tucker, Jaimey D. Brindley, Amanda A. Dickman, Mark J. Hunter, C. Neil |
author_sort | Mothersole, David J. |
collection | PubMed |
description | The mature architecture of the photosynthetic membrane of the purple phototroph R hodobacter sphaeroides has been characterised to a level where an atomic‐level membrane model is available, but the roles of the putative assembly proteins LhaA and PucC in establishing this architecture are unknown. Here we investigate the assembly of light‐harvesting LH2 and reaction centre‐light‐harvesting1‐PufX (RC‐LH1‐PufX) photosystem complexes using spectroscopy, pull‐downs, native gel electrophoresis, quantitative mass spectrometry and fluorescence lifetime microscopy to characterise a series of lha A and puc C mutants. LhaA and PucC are important for specific assembly of LH1 or LH2 complexes, respectively, but they are not essential; the few LH1 subunits found in Δlha A mutants assemble to form normal RC‐LH1‐PufX core complexes showing that, once initiated, LH1 assembly round the RC is cooperative and proceeds to completion. LhaA and PucC form oligomers at sites of initiation of membrane invagination; LhaA associates with RCs, bacteriochlorophyll synthase (BchG), the protein translocase subunit YajC and the YidC membrane protein insertase. These associations within membrane nanodomains likely maximise interactions between pigments newly arriving from BchG and nascent proteins within the SecYEG‐SecDF‐YajC‐YidC assembly machinery, thereby co‐ordinating pigment delivery, the co‐translational insertion of LH polypeptides and their folding and assembly to form photosynthetic complexes. |
format | Online Article Text |
id | pubmed-4949548 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2015 |
publisher | John Wiley and Sons Inc. |
record_format | MEDLINE/PubMed |
spelling | pubmed-49495482016-07-28 PucC and LhaA direct efficient assembly of the light‐harvesting complexes in Rhodobacter sphaeroides Mothersole, David J. Jackson, Philip J. Vasilev, Cvetelin Tucker, Jaimey D. Brindley, Amanda A. Dickman, Mark J. Hunter, C. Neil Mol Microbiol Research Articles The mature architecture of the photosynthetic membrane of the purple phototroph R hodobacter sphaeroides has been characterised to a level where an atomic‐level membrane model is available, but the roles of the putative assembly proteins LhaA and PucC in establishing this architecture are unknown. Here we investigate the assembly of light‐harvesting LH2 and reaction centre‐light‐harvesting1‐PufX (RC‐LH1‐PufX) photosystem complexes using spectroscopy, pull‐downs, native gel electrophoresis, quantitative mass spectrometry and fluorescence lifetime microscopy to characterise a series of lha A and puc C mutants. LhaA and PucC are important for specific assembly of LH1 or LH2 complexes, respectively, but they are not essential; the few LH1 subunits found in Δlha A mutants assemble to form normal RC‐LH1‐PufX core complexes showing that, once initiated, LH1 assembly round the RC is cooperative and proceeds to completion. LhaA and PucC form oligomers at sites of initiation of membrane invagination; LhaA associates with RCs, bacteriochlorophyll synthase (BchG), the protein translocase subunit YajC and the YidC membrane protein insertase. These associations within membrane nanodomains likely maximise interactions between pigments newly arriving from BchG and nascent proteins within the SecYEG‐SecDF‐YajC‐YidC assembly machinery, thereby co‐ordinating pigment delivery, the co‐translational insertion of LH polypeptides and their folding and assembly to form photosynthetic complexes. John Wiley and Sons Inc. 2015-11-05 2016-01 /pmc/articles/PMC4949548/ /pubmed/26419219 http://dx.doi.org/10.1111/mmi.13235 Text en © 2015 The Authors. Molecular Microbiology published by John Wiley & Sons Ltd. This is an open access article under the terms of the Creative Commons Attribution (http://creativecommons.org/licenses/by/4.0/) License, which permits use, distribution and reproduction in any medium, provided the original work is properly cited. |
spellingShingle | Research Articles Mothersole, David J. Jackson, Philip J. Vasilev, Cvetelin Tucker, Jaimey D. Brindley, Amanda A. Dickman, Mark J. Hunter, C. Neil PucC and LhaA direct efficient assembly of the light‐harvesting complexes in Rhodobacter sphaeroides |
title | PucC and LhaA direct efficient assembly of the light‐harvesting complexes in Rhodobacter sphaeroides
|
title_full | PucC and LhaA direct efficient assembly of the light‐harvesting complexes in Rhodobacter sphaeroides
|
title_fullStr | PucC and LhaA direct efficient assembly of the light‐harvesting complexes in Rhodobacter sphaeroides
|
title_full_unstemmed | PucC and LhaA direct efficient assembly of the light‐harvesting complexes in Rhodobacter sphaeroides
|
title_short | PucC and LhaA direct efficient assembly of the light‐harvesting complexes in Rhodobacter sphaeroides
|
title_sort | pucc and lhaa direct efficient assembly of the light‐harvesting complexes in rhodobacter sphaeroides |
topic | Research Articles |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4949548/ https://www.ncbi.nlm.nih.gov/pubmed/26419219 http://dx.doi.org/10.1111/mmi.13235 |
work_keys_str_mv | AT mothersoledavidj puccandlhaadirectefficientassemblyofthelightharvestingcomplexesinrhodobactersphaeroides AT jacksonphilipj puccandlhaadirectefficientassemblyofthelightharvestingcomplexesinrhodobactersphaeroides AT vasilevcvetelin puccandlhaadirectefficientassemblyofthelightharvestingcomplexesinrhodobactersphaeroides AT tuckerjaimeyd puccandlhaadirectefficientassemblyofthelightharvestingcomplexesinrhodobactersphaeroides AT brindleyamandaa puccandlhaadirectefficientassemblyofthelightharvestingcomplexesinrhodobactersphaeroides AT dickmanmarkj puccandlhaadirectefficientassemblyofthelightharvestingcomplexesinrhodobactersphaeroides AT huntercneil puccandlhaadirectefficientassemblyofthelightharvestingcomplexesinrhodobactersphaeroides |