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Comparison of Double‐Stranded RNA Binding Motifs between Different Organisms
Author(s) -
Brown Courtney L.,
Macbeth Mark R.
Publication year - 2020
Publication title -
the faseb journal
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.709
H-Index - 277
eISSN - 1530-6860
pISSN - 0892-6638
DOI - 10.1096/fasebj.2020.34.s1.00554
Subject(s) - adar , rna , rna silencing , biology , rna editing , transcription (linguistics) , genetics , messenger rna , dna , computational biology , microbiology and biotechnology , gene , rna interference , linguistics , philosophy
Transmission of genetic information from DNA to protein passes through a messenger‐RNA intermediate. This mRNA is extensively processed after transcription, and one enzyme that does so is a denosine d e a minase that acts on R NA (ADAR). ADARs catalyze the deamination of adenosines into inosines on double‐stranded RNA (dsRNA) substrates, ultimately leading to a mutation in their encoded protein. These mutations are essential not only for a properly functioning nervous system, but for survival. The ADAR enzyme is composed of two domains: a catalytic domain and an RNA binding domain that consists of one or more double‐stranded RNA binding motifs (dsRBMs). Determining the structures of these dsRBMs could lead to insight on the substrate specificity observed in ADARs, as it is known they are not sequence specific. To do so, dsRBMs from various organisms were subcloned into an expression plasmid, expressed, purified, re‐folded, and will be crystallized to determine their 3D structure by X‐ray diffraction. The structures of these dsRBMs from different organisms will be compared for similarities and differences to gain understanding into the mechanism by which they recognize their specific substrates. Support or Funding Information Butler Summer Institute (CLB, Summer 2019)Holcomb Awards Committee Grant (MRM, 2019)