| Conserved Residues at the Mtr4 C-Terminus Coordinate Helicase Activity and Exosome Interactions. | Conserved Residues at the Mtr4 C-Terminus Coordinate Helicase Activity and Exosome Interactions.
Yim MK, Stuart CJ, Pond MI, van Hoof A, Johnson SJ., Free PMC Article | 01/4/2024 |
| In vivo characterization of the critical interaction between the RNA exosome and the essential RNA helicase Mtr4 in Saccharomyces cerevisiae. | In vivo characterization of the critical interaction between the RNA exosome and the essential RNA helicase Mtr4 in Saccharomyces cerevisiae.
Sterrett MC, Farchi D, Strassler SE, Boise LH, Fasken MB, Corbett AH., Free PMC Article | 08/10/2023 |
| Purification and characterization of Mtr4 and TRAMP from S. cerevisiae. | Purification and characterization of Mtr4 and TRAMP from S. cerevisiae.
Yim MK, Denson JM, Gold MD, Johnson SJ. | 08/27/2022 |
| Hydrogen-deuterium exchange mass spectrometry of Mtr4 with diverse RNAs reveals substrate-dependent dynamics and interfaces in the arch. | Hydrogen-deuterium exchange mass spectrometry of Mtr4 with diverse RNAs reveals substrate-dependent dynamics and interfaces in the arch.
Zhang N, Olsen KJ, Ball D, Johnson SJ, D'Arcy S., Free PMC Article | 05/14/2022 |
| Structure of the Maturing 90S Pre-ribosome in Association with the RNA Exosome. | Structure of the Maturing 90S Pre-ribosome in Association with the RNA Exosome.
Lau B, Cheng J, Flemming D, La Venuta G, Berninghausen O, Beckmann R, Hurt E. | 02/6/2021 |
| Mpp6-exosomes can recruit Mtr4, while Mpp6 and Rrp47 each contribute to Mtr4-dependent RNA decay, with maximal Mtr4-dependent decay observed with both cofactors. | Structure and reconstitution of yeast Mpp6-nuclear exosome complexes reveals that Mpp6 stimulates RNA decay and recruits the Mtr4 helicase.
Wasmuth EV, Zinder JC, Zattas D, Das M, Lima CD., Free PMC Article | 05/5/2018 |
| report the 3.2 A resolution crystal structure of S. cerevisiae Mtr4 bound to the interacting region of Nop53, revealing how the KOW domain of the helicase recognizes the AIM sequence of Nop53 with a network of hydrophobic and electrostatic interactions | Structural insights into the interaction of the nuclear exosome helicase Mtr4 with the preribosomal protein Nop53.
Falk S, Tants JN, Basquin J, Thoms M, Hurt E, Sattler M, Conti E., Free PMC Article | 12/9/2017 |
| Rrp41 mutations blocked substrate passage through the channel to Rrp44 only for cytoplasmic mRNAs, supporting the predicted widening of the lumen in the Rrp6-associated.Many exosome substrates exhibited clear preferences for a specific path to Rrp44. Both threading and direct access routes involve the RNA helicase Mtr4 | Transcriptome-wide analysis of alternative routes for RNA substrates into the exosome complex.
Delan-Forino C, Schneider C, Tollervey D., Free PMC Article | 04/29/2017 |
| Mtr4p structural domain mutants in the helicase core reduced Mtr4p RNA binding, ATPase activity and unwinding activity in vitro. | Mutations in Mtr4 Structural Domains Reveal Their Important Role in Regulating tRNAiMet Turnover in Saccharomyces cerevisiae and Mtr4p Enzymatic Activities In Vitro.
Li Y, Burclaff J, Anderson JT., Free PMC Article | 07/30/2016 |
| Study reports the identification of adaptor proteins that recruit the exosome-associated helicase, Mtr4, to unique RNA substrates. Nop53, the yeast homolog of the tumor suppressor PICT1, targets Mtr4 to pre-ribosomal particles for exosome-mediated processing, while a second adaptor Utp18 recruits Mtr4 to cleaved rRNA fragments destined for degradation by the exosome. | The Exosome Is Recruited to RNA Substrates through Specific Adaptor Proteins.
Thoms M, Thomson E, Baßler J, Gnädig M, Griesel S, Hurt E. | 11/28/2015 |
| Mtr4 is linked to the core exosome through its binding to the Rrp6 - Rrp47 composite surface. | The exosome-binding factors Rrp6 and Rrp47 form a composite surface for recruiting the Mtr4 helicase.
Schuch B, Feigenbutz M, Makino DL, Falk S, Basquin C, Mitchell P, Conti E., Free PMC Article | 07/25/2015 |
| The studt demonstrates that the ratchet helix modulates helicase activity and suggest that the arch domain plays a previously unrecognized role in unwinding substrates. | The Mtr4 ratchet helix and arch domain both function to promote RNA unwinding.
Taylor LL, Jackson RN, Rexhepaj M, King AK, Lott LK, van Hoof A, Johnson SJ., Free PMC Article | 05/16/2015 |
| The RNA binding part of the Mtr4p arch, the KOW domain, as the essential component for TRAMP-mediated exosome activation. | Air2p is critical for the assembly and RNA-binding of the TRAMP complex and the KOW domain of Mtr4p is crucial for exosome activation.
Holub P, Lalakova J, Cerna H, Pasulka J, Sarazova M, Hrazdilova K, Arce MS, Hobor F, Stefl R, Vanacova S., Free PMC Article | 10/6/2012 |
| Data show that the unwinding activity of Mtr4p is significantly stimulated by Trf4p/Air2p, but the stimulation of Mtr4p does not depend on ongoing polyadenylation. | RNA unwinding by the Trf4/Air2/Mtr4 polyadenylation (TRAMP) complex.
Jia H, Wang X, Anderson JT, Jankowsky E., Free PMC Article | 08/18/2012 |
| Air1 zinc knuckles 4 and 5 and a conserved IWRXY motif are critical for the function and integrity of the Trf4/5-Air1/2-Mtr4 polyadenylation (TRAMP) RNA quality control complex. | Air1 zinc knuckles 4 and 5 and a conserved IWRXY motif are critical for the function and integrity of the Trf4/5-Air1/2-Mtr4 polyadenylation (TRAMP) RNA quality control complex.
Fasken MB, Leung SW, Banerjee A, Kodani MO, Chavez R, Bowman EA, Purohit MK, Rubinson ME, Rubinson EH, Corbett AH., Free PMC Article | 12/17/2011 |
| Data establish Mtr4p as a critical regulator of polyadenylation by TRAMP and reveal that an RNA helicase can control the activity of another enzyme in a highly complex fashion and in response to features in RNA. | The RNA helicase Mtr4p modulates polyadenylation in the TRAMP complex.
Jia H, Wang X, Liu F, Guenther UP, Srinivasan S, Anderson JT, Jankowsky E., Free PMC Article | 08/20/2011 |
| Unique properties of the Mtr4-polyA interaction indicate that one role of Mtr4 is to discriminate between substrates and thereby maintain contact with the short polyadenylated sequences that signal degradation. | Unique properties of the Mtr4p-poly(A) complex suggest a role in substrate targeting.
Bernstein J, Ballin JD, Patterson DN, Wilson GM, Toth EA., Free PMC Article | 01/15/2011 |
| Data show that Mtr4 has evolved specific structural and surface features to perform its multiple functions. | Structural analysis reveals the characteristic features of Mtr4, a DExH helicase involved in nuclear RNA processing and surveillance.
Weir JR, Bonneau F, Hentschel J, Conti E., Free PMC Article | 09/6/2010 |
| The crystal structure reveals a new arch-like domain that is specific to Mtr4 and Ski2 (the cytosolic homologue of Mtr4) and is required for rRNA processing. | The crystal structure of Mtr4 reveals a novel arch domain required for rRNA processing.
Jackson RN, Klauer AA, Hintze BJ, Robinson H, van Hoof A, Johnson SJ., Free PMC Article | 08/9/2010 |
| Data suggest that neither the poly(A) polymerase activity of Trf4 nor the helicase activity of Mtr4 plays a role in the enhancement of RNA degradation by the nuclear exosome component Rrp6. | TRAMP complex enhances RNA degradation by the nuclear exosome component Rrp6.
Callahan KP, Butler JS., Free PMC Article | 04/12/2010 |
| Mtr4p displays a marked preference for binding to poly(A) RNA relative to an oligoribonucleotide of the same length and a random sequence. | Characterization of the essential activities of Saccharomyces cerevisiae Mtr4p, a 3'->5' helicase partner of the nuclear exosome.
Bernstein J, Patterson DN, Wilson GM, Toth EA. | 01/21/2010 |