The zinc-finger antiviral protein recruits the RNA processing exosome to degrade the target mRNA

被引：230

作者：

Guo, Xuemin ^{[1
]}

Ma, Jing ^{[1
]}

Sun, Jing ^{[1
]}

Gao, Guangxia ^{[1
]}

机构：

[1] Chinese Acad Sci, Inst Biophys, Beijing 100101, Peoples R China

来源：

PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA | 2007年 / 104卷 / 01期

关键词：

RNA degradation;

D O I：

10.1073/pnas.0607063104

中图分类号：

O [数理科学和化学]; P [天文学、地球科学]; Q [生物科学]; N [自然科学总论];

学科分类号：

07 ; 0710 ; 09 ;

摘要：

Zinc-finger antiviral protein (ZAP) is a host antiviral factor that specifically inhibits the replication of Moloney murine leukemia virus (MLV) and Sindbis virus (SIN) by preventing accumulation of the viral mRNA in the cytoplasm. in previous studies, we demonstrated that ZAP directly binds to its specific target mRNAs. In this article, we provide evidence indicating that ZAP recruits the RNA processing exosome to degrade the target RNA. ZAP comigrated with the exosome in sucrose or glycerol velocity gradient centrifugation. Immunoprecipitation of ZAP coprecipitated the exosome components. In vitro pull-down assays indicated that ZAP directly interacted with the exosome component hRrp46p and that the binding region of ZAP was mapped to amino acids 224-254. Depletion of the exosome component hRrp41p or hRrp46p with small interfering RNA significantly reduced ZAP's destabilizing activity. These findings suggest that ZAP is a trans-acting factor that modulates mRNA stability.

引用

页码：151 / 156

页数：6

共 74 条

[1] The yeast exosome and human PM-Scl are related complexes of 3′→5′ exonucleases [J].

Allmang, C ;

Petfalski, E ;

Podtelejnikov, A ;

Mann, M ;

Tollervey, D ;

Mitchell, P .

GENES & DEVELOPMENT, 1999, 13 (16) :2148-2158

[2] Functions of the exosome in rRNA, snoRNA and snRNA synthesis [J].

Allmang, C ;

Kufel, J ;

Chanfreau, G ;

Mitchell, P ;

Petfalski, E ;

Tollervey, D .

EMBO JOURNAL, 1999, 18 (19) :5399-5410

[3] Degradation of ribosomal RNA precursors by the exosome [J].

Allmang, Christine ;

Mitchell, Philip ;

Petfalski, Elisabeth ;

Tollervey, David .

NUCLEIC ACIDS RESEARCH, 2000, 28 (08) :1684-1691

[4] A complex prediction:: three-dimensional model of the yeast exosome [J].

Aloy, P ;

Ciccarelli, FD ;

Leutwein, C ;

Gavin, AC ;

Superti-Furga, G ;

Bork, P ;

Böttcher, B ;

Russell, RB .

EMBO REPORTS, 2002, 3 (07) :628-635

[5] The 3′ to 5′ degradation of yeast mRNAs is a general mechanism for mRNA turnover that requires the SKI2 DEVH box protein and 3′ to 5′ exonucleases of the exosome complex [J].

Anderson, JSJ ;

Parker, R .

EMBO JOURNAL, 1998, 17 (05) :1497-1506

[6] ARED 2.0: an update of AU-rich element mRNA database [J].

Bakheet, T ;

Williams, BRG ;

Khabar, KSA .

NUCLEIC ACIDS RESEARCH, 2003, 31 (01) :421-423

[7] ARED: human AU-rich element-containing mRNA database reveals an unexpectedly diverse functional repertoire of encoded proteins [J].

Bakheet, T ;

Frevel, M ;

Williams, BRG ;

Greer, W ;

Khabar, KSA .

NUCLEIC ACIDS RESEARCH, 2001, 29 (01) :246-254

[8] Post-transcriptional regulation of gene expression by degradation of messenger RNAs [J].

Bevilacqua, A ;

Ceriani, MC ;

Capaccioli, S ;

Nicolin, A .

JOURNAL OF CELLULAR PHYSIOLOGY, 2003, 195 (03) :356-372

[9]

BHARUCHA AD, 1992, METHOD ENZYMOL, V216, P168

[10] Expression of the zinc-finger antiviral protein inhibits alphavirus replication [J].

Bick, MJ ;

Carroll, JWN ;

Gao, GX ;

Goff, SP ;

Rice, CM ;

MacDonald, MR .

JOURNAL OF VIROLOGY, 2003, 77 (21) :11555-11562

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