gopubmed logo
 
find other proteinsAll proteins
GoPubMed Proteins lists recent and important papers and reviews for proteins. Page last changed on 08 Dec 2016.

MTR4 Mtr4p

Mtr4p, Mtr4, DOB1, KIAA0052
Top mentioned proteins: DR3, CAN, POLYMERASE, ATPase, ACID
Papers on Mtr4p
Fluctuation of Arabidopsis seed dormancy with relative humidity and temperature during dry storage.
New
Bailly et al., Paris, France. In J Exp Bot, Jan 2016
Seeds of the wild type Col-0 and of two mutants displaying low and high levels of dormancy, cat2-1 and mtr4-1, respectively, were stored at harvest in 24 different environments including a combination of eight relative humidities, from 1 to 85%, and four temperatures (10, 15, 20, and 25 °C).
AAA-ATPase NVL2 acts on MTR4-exosome complex to dissociate the nucleolar protein WDR74.
New
Nagahama et al., Tokyo, Japan. In Biochem Biophys Res Commun, Dec 2015
We previously showed that NVL2 interacts with RNA processing/degradation machinery containing an RNA helicase MTR4/DOB1 and an exonuclease complex, nuclear exosome, and involved in the biogenesis of 60S ribosomal subunits.
NVL2, a nucleolar AAA-ATPase, is associated with the nuclear exosome and is involved in pre-rRNA processing.
New
Nagahama et al., Tokushima, Japan. In Biochem Biophys Res Commun, Sep 2015
We previously showed the interaction of NVL2 with a DExD/H-box RNA helicase MTR4/DOB1, which is a known cofactor for an exoribonuclease complex, the exosome.
Immature large ribosomal subunits containing the 7S pre-rRNA can engage in translation in Saccharomyces cerevisiae.
de la Cruz et al., Sevilla, Spain. In Rna Biol, 2014
In this study, we describe that cells harbouring the dob1-1 allele, encoding a mutated version of the exosome-assisting RNA helicase Mtr4, accumulate otherwise nuclear pre-60S ribosomal particles containing the 7S pre-rRNA in the cytoplasm.
The RNA helicases AtMTR4 and HEN2 target specific subsets of nuclear transcripts for degradation by the nuclear exosome in Arabidopsis thaliana.
Gagliardi et al., Strasbourg, France. In Plos Genet, 2014
In both yeast and human, all nuclear functions of the exosome require the RNA helicase MTR4.
The roles of SSU processome components and surveillance factors in the initial processing of human ribosomal RNA.
Watkins et al., In Rna, 2014
Interestingly, we show that the RNA surveillance factors XRN2 and MTR4 are also involved in A' cleavage in humans.
Cotranscriptional recruitment of yeast TRAMP complex to intronic sequences promotes optimal pre-mRNA splicing.
Wong et al., Hong Kong, Hong Kong. In Nucleic Acids Res, 2014
In budding yeast, a number of these unwanted RNA transcripts, including spliced-out introns, are first recognized by the nuclear exosome cofactor Trf4/5p-Air1/2p-Mtr4p polyadenylation (TRAMP) complex before subsequent nuclear-exosome-mediated degradation.
Certain adenylated non-coding RNAs, including 5' leader sequences of primary microRNA transcripts, accumulate in mouse cells following depletion of the RNA helicase MTR4.
Anderson et al., Bethesda, United States. In Plos One, 2013
We have used a small interfering RNA in mouse N2A cells to target the homolog of a yeast protein that functions in RNA surveillance (Mtr4p).
Air2p is critical for the assembly and RNA-binding of the TRAMP complex and the KOW domain of Mtr4p is crucial for exosome activation.
GeneRIF
Vanacova et al., Brno, Czech Republic. In Nucleic Acids Res, 2012
The RNA binding part of the Mtr4p arch, the KOW domain, as the essential component for TRAMP-mediated exosome activation.
RNA unwinding by the Trf4/Air2/Mtr4 polyadenylation (TRAMP) complex.
GeneRIF
Jankowsky et al., Cleveland, United States. In Proc Natl Acad Sci U S A, 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.
microRNAs targeting DEAD-box helicases are involved in salinity stress response in rice (Oryza sativa L.).
Tuteja et al., New Delhi, India. In Bmc Plant Biol, 2011
The present miRNAs were predicted to target the OsABP (ATP-Binding Protein), OsDSHCT (DOB1/SK12/helY-like DEAD-box Helicase) and OsDBH (DEAD-Box Helicase) genes, included in the DEAD-box helicase family.
Polyadenylation-dependent control of long noncoding RNA expression by the poly(A)-binding protein nuclear 1.
Bachand et al., Sherbrooke, Canada. In Plos Genet, 2011
PABPN1-sensitive lncRNAs are targeted by the exosome and the RNA helicase MTR4/SKIV2L2; yet, the polyadenylation activity of TRF4-2, a putative human TRAMP subunit, appears to be dispensable for PABPN1-dependent regulation.
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.
GeneRIF
Corbett et al., Atlanta, United States. In J Biol Chem, 2011
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.
The RNA helicase Mtr4p modulates polyadenylation in the TRAMP complex.
Impact
GeneRIF
Jankowsky et al., Cleveland, United States. In Cell, 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.
Unique properties of the Mtr4p-poly(A) complex suggest a role in substrate targeting.
GeneRIF
Toth et al., Baltimore, United States. In Biochemistry, 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.
Biogenesis of the signal recognition particle.
Review
Brown et al., Newcastle upon Tyne, United Kingdom. In Biochem Soc Trans, 2010
In the present paper, the SRP assembly pathway is summarized, and evidence for the involvement of both the Rex1p and nuclear exosome nucleases and the TRAMP (Trf4-Air2-Mtr4p polyadenylation) adenylase in quality control of SRP RNA is discussed.
RNA degradation by the exosome is promoted by a nuclear polyadenylation complex.
Impact
Tollervey et al., Edinburgh, United Kingdom. In Cell, 2005
This work identifies a nuclear polyadenylation complex containing a known exosome cofactor, the RNA helicase Mtr4p; a poly(A) polymerase, Trf4p; and a zinc knuckle protein, Air2p.
Musing on the structural organization of the exosome complex.
Review
Tollervey et al., Edinburgh, United Kingdom. In Nat Struct Biol, 2000
Both processing and degradative activities of the exosome depend on additional cofactors, notably the putative RNA helicases Mtr4p and Ski2p.
share on facebooktweetadd +1mail to friends