Abstract：
:Sm and Sm-like (Lsm) proteins are considered as an evolutionary conserved family involved in RNA metabolism in organisms from bacteria and archaea to human. Currently, the function of Sm-like archaeal proteins (SmAP) is not well understood. Here, we report the crystal structures of SmAP proteins from Sulfolobus acidocaldarius and Methanococcus vannielii and a comparative analysis of their RNA-binding sites. Our data show that these SmAPs have only a uridine-specific RNA-binding site, unlike their bacterial homolog Hfq, which has three different RNA-binding sites. Moreover, variations in the amino acid composition of the U-binding sites of the two SmAPs lead to a difference in protein affinity for oligo(U) RNA. Surface plasmon resonance data and nucleotide-binding analysis confirm the high affinity of SmAPs for uridine nucleotides and oligo(U) RNA and the reduced affinity for adenines, guanines, cytidines and corresponding oligo-RNAs. In addition, we demonstrate that MvaSmAP1 and SacSmAP2 are capable of melting an RNA hairpin and, apparently, promote its interaction with complementary RNA.
journal_name
Biochimiejournal_title
Biochimieauthors
Lekontseva N,Mikhailina A,Fando M,Kravchenko O,Balobanov V,Tishchenko S,Nikulin Adoi
10.1016/j.biochi.2020.05.001subject
Has Abstractpub_date
2020-08-01 00:00:00pages
1-12eissn
0300-9084issn
1638-6183pii
S0300-9084(20)30097-3journal_volume
175pub_type
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