Solution structure of protein SRP19 of Archaeoglobus fulgidus signal recognition particle

Journal of Molecular Biology
O N PakhomovaA P Hinck

Abstract

Protein SRP19 is an essential RNA-binding component of the signal recognition particle (SRP) in Archaea and Eucarya. A three-dimensional solution structure of the 104 residue SRP19 from the hyperthermophilic archaeon Archaeoglobus fulgidus, designated as Af19, was determined by NMR spectroscopy. Af19 contains three beta-strands, two alpha-helical regions, arranged in a betaalphabetabetaalpha topology, a 3(10) helix, and a disordered C-terminal tail. This fold is similar to the betaalphabetabetaalphabeta RNP motif present in numerous other RNA-binding proteins, which engage their cognate RNAs using conserved sequence motifs present within beta-strands 1 and 3. Mutagenesis studies of human SRP19, however, reveal the major contact sites with SRP RNA reside within loops 1, 3, and 4. These contacts were verified by the crystal structure of human SRP19 complexed to SRP RNA helix 6 reported subsequent to the submission of the manuscript. The crystal structure also reveals that, unlike canonical RNP motifs, SRP19 does not engage specific RNA bases through conserved sequence motifs present within beta-strands 1 and 3. Instead, SRP19 uses residues both within and flanking beta-strand 1 to stabilize the complex through direct and indirect...Continue Reading

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Citations

Aug 13, 2004·Philosophical Transactions of the Royal Society of London. Series B, Biological Sciences·Albert Bolhuis
Jun 11, 2004·Annual Review of Biochemistry·Jennifer A Doudna, Robert T Batey
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Dec 3, 2016·Current Microbiology·Sayandeep GuptaAbhrajyoti Ghosh
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Jun 12, 2021·Biochemical and Biophysical Research Communications·Sayandeep GuptaAbhrajyoti Ghosh
Mar 30, 2010·Biochimica Et Biophysica Acta·Doron Calo, Jerry Eichler

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