A direct interaction between DCP1 and XRN1 couples mRNA decapping to 5′ exonucleolytic degradation

被引：133

作者：

Braun, Joerg E. ^{[1
]}

Truffault, Vincent ^{[1
]}

Boland, Andreas ^{[1
]}

Huntzinger, Eric ^{[1
]}

Chang, Chung-Te ^{[1
]}

Haas, Gabrielle ^{[1
]}

Weichenrieder, Oliver ^{[1
]}

Coles, Murray ^{[1
]}

Izaurralde, Elisa ^{[1
]}

机构：

[1] Max Planck Inst Dev Biol, Dept Biochem, Tubingen, Germany

来源：

NATURE STRUCTURAL & MOLECULAR BIOLOGY | 2012年 / 19卷 / 12期

关键词：

MOLECULAR-STRUCTURE DETERMINATION; DOMAIN-PEPTIDE COMPLEX; N-TERMINAL DOMAIN; EVH1; DOMAIN; PROCESSING BODY; POLYPROLINE RECOGNITION; STRUCTURE VALIDATION; CHEMICAL-SHIFT; XPLOR-NIH; DEADENYLATION;

D O I：

10.1038/nsmb.2413

中图分类号：

Q5 [生物化学]; Q7 [分子生物学];

学科分类号：

071010 ; 081704 ;

摘要：

The removal of the mRNA 5' cap structure by the decapping enzyme DCP2 leads to rapid 5'-> 3' mRNA degradation by XRN1, suggesting that the two processes are coordinated, but the coupling mechanism is unknown. DCP2 associates with the decapping activators EDC4 and DCP1. Here we show that XRN1 directly interacts with EDC4 and DCP1 in human and Drosophila melanogaster cells, respectively. In D. melanogaster cells, this interaction is mediated by the DCP1 EVH1 domain and a DCP1-binding motif (DBM) in the XRN1 C-terminal region. The NMR structure of the DCP1 EVH1 domain bound to the DBM reveals that the peptide docks at a conserved aromatic cleft, which is used by EVH1 domains to recognize proline-rich ligands. Our findings reveal a role for XRN1 in decapping and provide a molecular basis for the coupling of decapping to 5'-> 3' mRNA degradation.

引用

页码：1324 / +

页数：10

共 51 条

[1] Dual epitope recognition by the VASP EVH1 domain modulates polyproline ligand specificity and binding affinity [J].

Ball, LJ ;

Kühne, R ;

Hoffmann, B ;

Häfner, A ;

Schmieder, P ;

Volkmer-Engert, R ;

Hof, M ;

Wahl, M ;

Schneider-Mergener, J ;

Walter, U ;

Oschkinat, H ;

Jarchau, T .

EMBO JOURNAL, 2000, 19 (18) :4903-4914

[2] EVH 1 domains: structure, function and interactions [J].

Ball, LJ ;

Jarchau, T ;

Oschkinat, H ;

Walter, U .

FEBS LETTERS, 2002, 513 (01) :45-52

[3] The N-terminal domain of Homer/Vesl is a new class II EVH1 domain [J].

Barzik, M ;

Carl, UD ;

Schubert, WD ;

Frank, R ;

Wehland, J ;

Heinz, DW .

JOURNAL OF MOLECULAR BIOLOGY, 2001, 309 (01) :155-169

[4] MRNA degradation by miRNAs and GW182 requires both CCR4:NOT deadenylase and DCP1:DCP2 decapping complexes [J].

Behm-Ansmant, Isabelle ;

Rehwinkel, Jan ;

Doerks, Tobias ;

Stark, Alexander ;

Bork, Peer ;

Izaurralde, Elisa .

GENES & DEVELOPMENT, 2006, 20 (14) :1885-1898

[5] Structure of the Homer EVH1 domain-peptide complex reveals a new twist in polyproline recognition [J].

Beneken, J ;

Tu, JC ;

Xiao, B ;

Nuriya, M ;

Yuan, JP ;

Worley, PF ;

Leahy, DJ .

NEURON, 2000, 26 (01) :143-154

[6] Identification and characterization of protein interactions in the mammalian mRNA processing body using a novel two-hybrid assay [J].

Bloch, Donald B. ;

Nobre, Rita A. ;

Bernstein, Gillian A. ;

Yang, Wei-Hong .

EXPERIMENTAL CELL RESEARCH, 2011, 317 (15) :2183-2199

[7] Dcp1 links coactivators of mRNA decapping to Dcp2 by proline recognition [J].

Borja, Mark S. ;

Piotukh, Kirill ;

Freund, Christian ;

Gross, John D. .

RNA, 2011, 17 (02) :278-290

[8] A Sm-like protein complex that participates in mRNA degradation [J].

Bouveret, E ;

Rigaut, G ;

Shevchenko, A ;

Wilm, M ;

Séraphin, B .

EMBO JOURNAL, 2000, 19 (07) :1661-1671

[9] GW182 Proteins Directly Recruit Cytoplasmic Deadenylase Complexes to miRNA Targets [J].

Braun, Joerg E. ;

Huntzinger, Eric ;

Fauser, Maria ;

Izaurralde, Elisa .

MOLECULAR CELL, 2011, 44 (01) :120-133

[10] Aromatic and basic residues within the EVH1 domain of VASP specify its interaction with proline-rich ligands [J].

Carl, UD ;

Pollmann, M ;

Orr, E ;

Gertler, FB ;

Chakraborty, T ;

Wehland, J .

CURRENT BIOLOGY, 1999, 9 (13) :715-718

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