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The structure of a highly-conserved picocyanobacterial protein reveals a Tudor domain with an RNA-binding function.
- Source :
-
The Journal of biological chemistry [J Biol Chem] 2019 Sep 27; Vol. 294 (39), pp. 14333-14344. Date of Electronic Publication: 2019 Aug 07. - Publication Year :
- 2019
-
Abstract
- Cyanobacteria of the Prochlorococcus and marine Synechococcus genera are the most abundant photosynthetic microbes in the ocean. Intriguingly, the genomes of these bacteria are strongly divergent even within each genus, both in gene content and at the amino acid level of the encoded proteins. One striking exception to this is a 62-amino-acid protein, termed P rochlorococcus / S ynechococcush yper- c onserved p rotein (PSHCP). PSHCP is not only found in all sequenced Prochlorococcus and marine Synechococcus genomes, but it is also nearly 100% identical in its amino acid sequence across all sampled genomes. Such universal distribution and sequence conservation suggest an essential cellular role of PSHCP in these bacteria. However, its function is unknown. Here, we used NMR spectroscopy to determine its structure, finding that 53 of the 62 amino acids in PSHCP form a Tudor domain, whereas the remainder of the protein is disordered. NMR titration experiments revealed that PSHCP has only a weak affinity for DNA, but an 18.5-fold higher affinity for tRNA, hinting at an involvement of PSHCP in translation. Isothermal titration calorimetry experiments further revealed that PSHCP also binds single-stranded, double-stranded, and hairpin RNAs. These results provide the first insight into the structure and function of PSHCP, suggesting that PSHCP appears to be an RNA-binding protein that can recognize a broad array of RNA molecules.<br /> (© 2019 Bauer et al.)
- Subjects :
- Bacterial Proteins metabolism
Conserved Sequence
Intrinsically Disordered Proteins metabolism
Prochlorococcus chemistry
Prochlorococcus metabolism
Protein Binding
RNA metabolism
RNA-Binding Proteins metabolism
Synechococcus chemistry
Synechococcus metabolism
Bacterial Proteins chemistry
Intrinsically Disordered Proteins chemistry
RNA-Binding Proteins chemistry
Tudor Domain
Subjects
Details
- Language :
- English
- ISSN :
- 1083-351X
- Volume :
- 294
- Issue :
- 39
- Database :
- MEDLINE
- Journal :
- The Journal of biological chemistry
- Publication Type :
- Academic Journal
- Accession number :
- 31391250
- Full Text :
- https://doi.org/10.1074/jbc.RA119.007938