Solution structure of the RNA-binding cold shock domain of the Chlamydomonas reinhardtii NAB1 protein and insights into RNA recognition

Sawyer, Anne L., Landsberg, Michael J., Ross, Ian L., Kruse, Olaf, Mobli, Mehdi and Hankamer, Ben (2015) Solution structure of the RNA-binding cold shock domain of the Chlamydomonas reinhardtii NAB1 protein and insights into RNA recognition. Biochemical Journal, 469 1: 97-106. doi:10.1042/BJ20150217


Author Sawyer, Anne L.
Landsberg, Michael J.
Ross, Ian L.
Kruse, Olaf
Mobli, Mehdi
Hankamer, Ben
Title Solution structure of the RNA-binding cold shock domain of the Chlamydomonas reinhardtii NAB1 protein and insights into RNA recognition
Formatted title
Solution structure of the RNA-binding cold shock domain of the Chlamydomonas reinhardtii NAB1 protein and insights into RNA recognition
Journal name Biochemical Journal   Check publisher's open access policy
ISSN 0264-6021
1470-8728
Publication date 2015-06-19
Year available 2015
Sub-type Article (original research)
DOI 10.1042/BJ20150217
Open Access Status Not Open Access
Volume 469
Issue 1
Start page 97
End page 106
Total pages 10
Place of publication London, United Kingdom
Publisher Portland Press
Language eng
Formatted 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).
Keyword Biochemistry & Molecular Biology
Biochemistry & Molecular Biology
Q-Index Code C1
Q-Index Status Confirmed Code
Grant ID DP130100346
DFG KR-1586/5-2
APP1047243
Institutional Status UQ

 
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Created: Sat, 02 May 2015, 00:42:28 EST by Susan Allen on behalf of Institute for Molecular Bioscience