SF1 and SF2 helicases: family matters

By Margaret E. Fairman-Williams, Ulf-Peter Guenther, Eckhard Jankowsky. Current Opinion in Structural Biology, 2010

925 citations recorded by the source corpus.

Helicases of the superfamily (SF) 1 and 2 are involved in virtually all aspects of RNA and DNA metabolism. SF1 and SF2 helicases share a catalytic core with high structural similarity, but different enzymes even within each superfamily perform a wide spectrum of distinct functions on diverse substrates. To rationalize similarities and differences between these helicases, we outline a classification based on protein families that are characterized by typical sequence, structural and mechanistic features. This classification complements and extends existing SF1 and SF2 helicase categorizations and highlights major structural and functional themes for these proteins. We discuss recent data in the context of this unifying view of SF1 and SF2 helicases.

Subfields: Molecular Biology

View Paper: https://www.semanticscholar.org/paper/cd0207ac0ec86d63c84c119da1e360ffb7f249c2

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In Molecular Biology

Citations in the corpus

Mechanisms and Functions of ATP-Dependent Chromatin-Remodeling Enzymes (2013, neutral): “The observations described above are consistent with the possibility that chromatin-remodeling activities evolved from a primitive DNA-translocating core (Fairman-Williams et al., 2010).”
Ribosome Biogenesis in the Yeast Saccharomyces cerevisiae (2013, background): “All but one, Mtr4, are SF2 family helicases characterized by DEAD- or DEAH-box protein motifs (referred to as DExD/H-box RNA helicases; Table 6) (Fairman-Williams et al. 2010).”
Structural insights into RNA recognition by RIG-I (2011, positive): “Although DEAD-box helicases are phylogenetically distinct from RLR proteins and they appear to bind ssRNA, DEAD-box proteins have a distinct motif IIa element that is similar to that observed in RLRs, and which contributes to dsRNA binding in the RIG-I structure (Fairman-Williams et al., 2010; Pyle,”
Structural basis for m7G recognition and 2′-O-methyl discrimination in capped RNAs by the innate immune receptor RIG-I (2016, neutral): “A major difference between the structures of Helicase-RD bound to 5′OH HP RNA compared with 5′ppp and Cap-0 RNAs lies in the helicase motif IVa, which is located in the Hel2 region of RIG-I (residues 664–685) and highly conserved in the SF2 family of helicases (18).”
Kinetic discrimination of self/non-self RNA by the ATPase activity of RIG-I and MDA5 (2015, neutral): “Sf2 helicase/ATPase family members, including RLRs, are characterized by the coupling of nucleic acid and ATP binding to a conformational switch which, in turn, can trigger various downstream functions [12, 26].”
A census of human RNA-binding proteins (2014, neutral): “409 families 1,049 families 68% (277) EIF4A1–3 22% (89) FMR1; FXR1; FXR2 9% (37) ELAVL1–4 1% (6) DAZL; DAZ1–4; BOLL”
A structure-based model of RIG-I activation. (2012, background): “RIG-I (retinoic acid-inducible gene-I, DDX58), MDA5 (melanoma-differentiation-associated gene 5, IFIH1), and LGP2 (Laboratory of Genetics and Physiology 2, DHX58)—form a family within superfamily 2 (SF2) RNA helicases and are closely related to DEAD-box helicases (Fairman-Williams et al. 2010).”
Unified mechanisms for self-RNA recognition by RIG-I Singleton-Merten syndrome variants (2018, background): “Results and discussion The RIG-I SMS variants C268F and E373A are located within SF2 ATP binding and hydrolysis motifs I and II, respectively, (Fairman-Williams et al., 2010) (Figure 1—figure supplement 1) and were previously shown to be constitutively active in reporter cells without any external d”
Structural basis for RNA translocation by DEAH-box ATPases (2019, background): “They all belong to the helicase superfamily 2 (SF2) and share at least eight conserved sequence motifs (motifs I, Ia, Ib, II, III, IV, V and VI) spread over two RecA-like domains that together form the helicase core (7).”