All experiments were performed by SK under supervision of RR. The paper was co-drafted by SK and RR. All authors approved the final version of the manuscript.”
“Background Helicases are encoded by a large fraction of prokaryotic and eukaryotic
genomes and are found in all organisms –from bacteria to humans– and in many viruses. These nucleic acid-dependent selleck screening library NTPases (preferentially ATPases) have the ability to unwind DNA or RNA duplex substrates; to unwind/separate the helical structure of double-stranded nucleic acids and, in some cases, to disrupt protein-nucleic acid interactions [1, 2]. DNA and RNA helicases are grouped into six superfamilies (SF). SF1 and SF2 do not form rings, whereas SF3 to SF6 comprise the ring-forming helicases . All eukaryotic RNA helicases belong to SF1 and SF2, whereas the ring-shaped RNA helicases are found in viruses  and bacteria [5, 6]. GDC-973 Functional groups for ATP binding and hydrolysis are highly conserved among SF1 and SF2 DNA and RNA helicases. In addition, these two superfamilies show high sequence similarity in their conserved regions, sharing
eight conserved motifs; and variations within these conserved motifs are used to distinguish between these very closely related families. The helicases from SF1 and SF2 are further divided into families, based on their sequence, structural, and mechanistic features [3, 7]. According to an excellent Sepantronium mw classification proposed by Jankowsky’s group, these helicases can be grouped into three families in the SF1 and nine families and one group in the SF2 . Although several helicase families Resveratrol contain both RNA and DNA helicases, six of these twelve families only contain RNA helicases (DEAD-box, DEAH-box, Ski2-like, RIG-I-like, NS3/NPH-II and Upf1-like families). As they are mainly composed by RNA helicases, these 6 families are termed “RNA helicase families”, and are often referred to as DExD/H proteins. In the SF1 and SF2 helicases, the conserved motifs are clustered in a “central” core region that spans about 350 to 400 amino acids (named “Helicase Core Domain” – HCD). By contrast,
the N- and C-terminal extensions of helicases are highly variable in size and composition. These regions are supposed to confer substrate specificity, comprising protein- and/or RNA-binding motifs that provide helicases with their capacity to be involved in multiple processes, and/or direct the helicases to their subcellular localization [9, 10]. Within these extensions helicases also contain accessory domains that can confer specific functions, as in the case of the bidentate RNase III enzyme Dicer . The conservation of these domains within a family is null; therefore, they are not used to define a typical group. RNA is involved in virtually all aspects of gene expression, playing important regulatory roles in biological reactions and making RNAs biologically important molecules required by all living organisms.