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Solution structure of the RNA-binding cold-shock domain of the Chlamydomonas reinhardtii NAB1 protein and insights into RNA recognition
- Source :
- Biochemical Journal. 469:97-106
- Publication Year :
- 2015
- Publisher :
- Portland Press Ltd., 2015.
-
Abstract
- Light-harvesting complex (LHC) proteins are among the most abundant proteins on Earth and play critical roles in photosynthesis, both in light capture and in photoprotective mechanisms. The Chlamydomonas reinhardtii nucleic acid-binding protein 1 (NAB1) is a negative regulator of LHC protein translation. Its N-terminal cold-shock domain (CSD) binds to a 13-nt element [CSD consensus sequence (CSDCS)] found in the mRNA of specific LHC proteins associated with Photosystem II (PSII), an interaction which regulates LHC expression and, consequently, PSII-associated antenna size, structure and function. In the present study, we elucidated the solution structure of the NAB1 CSD as determined by heteronuclear NMR. The CSD adopts a characteristic five-stranded anti parallel β-barrel fold. Upon addition of CSDCS RNA, a large number of NMR chemical shift perturbations were observed, corresponding primarily to surface-exposed residues within the highly conserved β2- and β3-strands in the canonical RNA-binding region, but also to residues on β-strand 5 extending the positive surface patch and the overall RNA-binding site. Additional chemical shift perturbations that accompanied RNA binding involved buried residues, suggesting that transcript recognition is accompanied by conformational change. Our results indicate that NAB1 associates with RNA transcripts through a mechanism involving its CSD that is conserved with mechanisms of sequence-specific nucleic acid recognition employed by ancestrally related bacterial cold-shock proteins (CSPs).
- Subjects :
- Conformational change
RNA-binding protein
Chlamydomonas reinhardtii
Biochemistry
cold-shock protein
light-harvesting complex (LHC) regulation
Consensus sequence
RNA, Messenger
translational repressor
Nuclear Magnetic Resonance, Biomolecular
Molecular Biology
Plant Proteins
magnetic resonance (NMR)
Messenger RNA
biology
RNA-Binding Proteins
RNA
Cell Biology
Cold-shock domain
biology.organism_classification
Protein Structure, Tertiary
nuclear
RNA, Plant
Nucleic acid
Biophysics
Subjects
Details
- ISSN :
- 14708728 and 02646021
- Volume :
- 469
- Database :
- OpenAIRE
- Journal :
- Biochemical Journal
- Accession number :
- edsair.doi.dedup.....1f82f870d9f1a0d968274e5be74586ee