at Google ScholarTitle data
Horn, Annemarie ; Hennig, Janosch ; Ahmed, Yasar L. ; Stier, Gunter ; Wild, Klemens ; Sattler, Michael ; Sinning, Irmgard:
Structural basis for cpSRP43 chromodomain selectivity and dynamics in Alb3 insertase interaction.
In: Nature Communications.
Vol. 6
(2015)
.
- 8875.
ISSN 2041-1723
DOI: https://doi.org/10.1038/ncomms9875
Abstract in another language
Canonical membrane protein biogenesis requires co-translational delivery of ribosome-associated proteins to the Sec translocase and depends on the signal recognition particle (SRP) and its receptor (SR). In contrast, high-throughput delivery of abundant light-harvesting chlorophyll a,b-binding proteins (LHCPs) in chloroplasts to the Alb3 insertase occurs post-translationally via a soluble transit complex including the cpSRP43/cpSRP54 heterodimer (cpSRP). Here we describe the molecular mechanisms of tethering cpSRP to the Alb3 insertase by specific interaction of cpSRP43 chromodomain 3 with a linear motif in the Alb3 C-terminal tail. Combining NMR spectroscopy, X-ray crystallography and biochemical analyses, we dissect the structural basis for selectivity of chromodomains 2 and 3 for their respective ligands cpSRP54 and Alb3, respectively. Negative cooperativity in ligand binding can be explained by dynamics in the chromodomain interface. Our study provides a model for membrane recruitment of the transit complex and may serve as a prototype for a functional gain by the tandem arrangement of chromodomains.
Further data
| Item Type: | Article in a journal |
|---|---|
| Refereed: | Yes |
| Institutions of the University: | Faculties > Faculty of Biology, Chemistry and Earth Sciences > Department of Chemistry > Chair Biochemistry IV - Biophysical Chemistry > Chair Biochemistry IV - Biophysical Chemistry - Univ.-Prof. Dr. Janosch Hennig Faculties Faculties > Faculty of Biology, Chemistry and Earth Sciences Faculties > Faculty of Biology, Chemistry and Earth Sciences > Department of Chemistry Faculties > Faculty of Biology, Chemistry and Earth Sciences > Department of Chemistry > Chair Biochemistry IV - Biophysical Chemistry Research Institutions > Central research institutes > Nordbayerisches Zentrum für NMR-Spektroskopie - NMR-Zentrum Research Institutions Research Institutions > Central research institutes |
| Result of work at the UBT: | No |
| DDC Subjects: | 500 Science > 540 Chemistry 500 Science > 570 Life sciences, biology |
| Date Deposited: | 07 Oct 2021 12:35 |
| Last Modified: | 21 Nov 2024 14:17 |
| URI: | https://eref.uni-bayreuth.de/id/eprint/67236 |