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Functional interaction of chloroplast SRP/FtsY with the ALB3 translocase in thylakoids
- Source :
- The Journal of Cell Biology
- Publication Year :
- 2003
- Publisher :
- Rockefeller University Press, 2003.
-
Abstract
- Integration of thylakoid proteins by the chloroplast signal recognition particle (cpSRP) posttranslational transport pathway requires the cpSRP, an SRP receptor homologue (cpFtsY), and the membrane protein ALB3. Similarly, Escherichia coli uses an SRP and FtsY to cotranslationally target membrane proteins to the SecYEG translocase, which contains an ALB3 homologue, YidC. In neither system are the interactions between soluble and membrane components well understood. We show that complexes containing cpSRP, cpFtsY, and ALB3 can be precipitated using affinity tags on cpSRP or cpFtsY. Stabilization of this complex with GMP-PNP specifically blocks subsequent integration of substrate (light harvesting chl a/b-binding protein [LHCP]), indicating that the complex occupies functional ALB3 translocation sites. Surprisingly, neither substrate nor cpSRP43, a component of cpSRP, was necessary to form a complex with ALB3. Complexes also contained cpSecY, but its removal did not inhibit ALB3 function. Furthermore, antibody bound to ALB3 prevented ALB3 association with cpSRP and cpFtsY and inhibited LHCP integration suggesting that a complex containing cpSRP, cpFtsY, and ALB3 must form for proper LHCP integration.
- Subjects :
- protein transport
signal recognition particle
receptors
membrane proteins
Arabidopsis proteins
Chloroplasts
Arabidopsis
Receptors, Cytoplasmic and Nuclear
Biology
Thylakoids
Transport Pathway
Article
Substrate Specificity
Chloroplast Proteins
03 medical and health sciences
Bacterial Proteins
Translocase
Signal recognition particle receptor
030304 developmental biology
0303 health sciences
Signal recognition particle
Arabidopsis Proteins
030302 biochemistry & molecular biology
Cell Biology
Chloroplast
Biochemistry
Membrane protein
Thylakoid
biology.protein
Biophysics
Signal Recognition Particle
Subjects
Details
- ISSN :
- 15408140 and 00219525
- Volume :
- 162
- Database :
- OpenAIRE
- Journal :
- Journal of Cell Biology
- Accession number :
- edsair.doi.dedup.....49d89e4da1e0ea1b9c0df39f1ea4a2a2
- Full Text :
- https://doi.org/10.1083/jcb.200307067