A Cyanobacterial Chlorophyll Synthase-HliD Complex Associates with the Ycf39 Protein and the YidC/Alb3 Insertase . Issue 3 (28th March 2014)
- Record Type:
- Journal Article
- Title:
- A Cyanobacterial Chlorophyll Synthase-HliD Complex Associates with the Ycf39 Protein and the YidC/Alb3 Insertase . Issue 3 (28th March 2014)
- Main Title:
- A Cyanobacterial Chlorophyll Synthase-HliD Complex Associates with the Ycf39 Protein and the YidC/Alb3 Insertase
- Authors:
- Chidgey, Jack W.
Linhartová, Markéta
Komenda, Josef
Jackson, Philip J.
Dickman, Mark J.
Canniffe, Daniel P.
Koník, Peter
Pilný, Jan
Hunter, C. Neil
Sobotka, Roman - Abstract:
- Abstract : Chlorophyll synthase attaches geranylgeraniol to the chlorophyll macrocycle and was used as bait to retrieve an enzymatically active complex comprising the synthase, the high-light-inducible protein HliD, Ycf39, and the YidC/Alb3 insertase. These data reveal a link between chlorophyll biosynthesis and Sec/YidC-dependent cotranslational insertion of nascent photosystem polypeptides into membranes. Abstract: Macromolecular membrane assemblies of chlorophyll-protein complexes efficiently harvest and trap light energy for photosynthesis. To investigate the delivery of chlorophylls to the newly synthesized photosystem apoproteins, a terminal enzyme of chlorophyll biosynthesis, chlorophyll synthase (ChlG), was tagged in the cyanobacterium Synechocystis PCC 6803 ( Synechocystis ) and used as bait in pull-down experiments. We retrieved an enzymatically active complex comprising ChlG and the high-light-inducible protein HliD, which associates with the Ycf39 protein, a putative assembly factor for photosystem II, and with the YidC/Alb3 insertase. 2D electrophoresis and immunoblotting also provided evidence for the presence of SecY and ribosome subunits. The isolated complex contained chlorophyll, chlorophyllide, and carotenoid pigments. Deletion of hliD elevated the level of the ChlG substrate, chlorophyllide, more than 6-fold; HliD is apparently required for assembly of FLAG-ChlG into larger complexes with other proteins such as Ycf39. These data reveal a link betweenAbstract : Chlorophyll synthase attaches geranylgeraniol to the chlorophyll macrocycle and was used as bait to retrieve an enzymatically active complex comprising the synthase, the high-light-inducible protein HliD, Ycf39, and the YidC/Alb3 insertase. These data reveal a link between chlorophyll biosynthesis and Sec/YidC-dependent cotranslational insertion of nascent photosystem polypeptides into membranes. Abstract: Macromolecular membrane assemblies of chlorophyll-protein complexes efficiently harvest and trap light energy for photosynthesis. To investigate the delivery of chlorophylls to the newly synthesized photosystem apoproteins, a terminal enzyme of chlorophyll biosynthesis, chlorophyll synthase (ChlG), was tagged in the cyanobacterium Synechocystis PCC 6803 ( Synechocystis ) and used as bait in pull-down experiments. We retrieved an enzymatically active complex comprising ChlG and the high-light-inducible protein HliD, which associates with the Ycf39 protein, a putative assembly factor for photosystem II, and with the YidC/Alb3 insertase. 2D electrophoresis and immunoblotting also provided evidence for the presence of SecY and ribosome subunits. The isolated complex contained chlorophyll, chlorophyllide, and carotenoid pigments. Deletion of hliD elevated the level of the ChlG substrate, chlorophyllide, more than 6-fold; HliD is apparently required for assembly of FLAG-ChlG into larger complexes with other proteins such as Ycf39. These data reveal a link between chlorophyll biosynthesis and the Sec/YidC-dependent cotranslational insertion of nascent photosystem polypeptides into membranes. We expect that this close physical linkage coordinates the arrival of pigments and nascent apoproteins to produce photosynthetic pigment-protein complexes with minimal risk of accumulating phototoxic unbound chlorophylls. … (more)
- Is Part Of:
- The Plant Cell. Volume 26:Issue 3(2014)
- Journal:
- The Plant Cell
- Issue:
- Volume 26:Issue 3(2014)
- Issue Display:
- Volume 26, Issue 3 (2014)
- Year:
- 2014
- Volume:
- 26
- Issue:
- 3
- Issue Sort Value:
- 2014-0026-0003-0000
- Page Start:
- 1267
- Page End:
- 1279
- Publication Date:
- 2014-03-28
- Journal URLs:
- http://www.oxfordjournals.org/ ↗
- DOI:
- 10.1105/tpc.114.124495 ↗
- Languages:
- English
- ISSNs:
- 1040-4651
- Deposit Type:
- Legaldeposit
- View Content:
- Available online (eLD content is only available in our Reading Rooms) ↗
- Physical Locations:
- British Library DSC - BLDSS-3PM
British Library HMNTS - ELD Digital store - Ingest File:
- 16316.xml