5FSW
RNA dependent RNA polymerase QDE-1 from Thielavia terrestris
Summary for 5FSW
| Entry DOI | 10.2210/pdb5fsw/pdb |
| Descriptor | RNA DEPENDENT RNA POLYMERASE QDE-1 (1 entity in total) |
| Functional Keywords | transferase, small rnas, qde-1 orthologues, evolution |
| Biological source | THIELAVIA TERRESTRIS |
| Total number of polymer chains | 4 |
| Total formula weight | 464235.44 |
| Authors | Qian, X.,Hamid, F.M.,El Sahili, A.,Darwis, D.A.,Wong, Y.H.,Bhushan, S.,Makeyev, E.V.,Lescar, J. (deposition date: 2016-01-08, release date: 2016-03-02, Last modification date: 2024-01-10) |
| Primary citation | Qian, X.,Hamid, F.M.,El Sahili, A.,Darwis, D.A.,Wong, Y.H.,Bhushan, S.,Makeyev, E.V.,Lescar, J. Functional Evolution in Orthologous Cell-Encoded RNA-Dependent RNA Polymerases J.Biol.Chem., 291:9295-, 2016 Cited by PubMed Abstract: Many eukaryotic organisms encode more than one RNA-dependent RNA polymerase (RdRP) that probably emerged as a result of gene duplication. Such RdRP paralogs often participate in distinct RNA silencing pathways and show characteristic repertoires of enzymatic activities in vitro However, to what extent members of individual paralogous groups can undergo functional changes during speciation remains an open question. We show that orthologs of QDE-1, an RdRP component of the quelling pathway in Neurospora crassa, have rapidly diverged in evolution at the amino acid sequence level. Analyses of purified QDE-1 polymerases from N. crassa (QDE-1(Ncr)) and related fungi, Thielavia terrestris (QDE-1(Tte)) and Myceliophthora thermophila (QDE-1(Mth)), show that all three enzymes can synthesize RNA, but the precise modes of their action differ considerably. Unlike their QDE-1(Ncr) counterpart favoring processive RNA synthesis, QDE-1(Tte) and QDE-1(Mth) produce predominantly short RNA copies via primer-independent initiation. Surprisingly, a 3.19 Å resolution crystal structure of QDE-1(Tte) reveals a quasisymmetric dimer similar to QDE-1(Ncr) Further electron microscopy analyses confirm that QDE-1(Tte) occurs as a dimer in solution and retains this status upon interaction with a template. We conclude that divergence of orthologous RdRPs can result in functional innovation while retaining overall protein fold and quaternary structure. PubMed: 26907693DOI: 10.1074/JBC.M115.685933 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (3.19 Å) |
Structure validation
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