The NFAR's (nuclear factors associated with dsRNA) Evolutionarily conserved members of the dsRNA binding protein family

被引:44
作者
Barber, Glen N. [1 ,2 ]
机构
[1] Univ Miami, Sch Med, Dept Med, Miami, FL 33136 USA
[2] Univ Miami, Sch Med, Sylvester Comprehens Canc Ctr, Miami, FL 33136 USA
关键词
NFAR; RNA export; RNA stabilization; translation; NF90; host defense; innate immunity; DOUBLE-STRANDED-RNA; ACTIVATED T-CELLS; MESSENGER-RNA; GENE-EXPRESSION; TRANSCRIPTION FACTOR; VIRUS-RNA; EXPORT; NF90; TRANSLATION; KINASE;
D O I
10.4161/rna.6.1.7565
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 dsRNA binding protein (DRBP) family comprise one or more evolutionarily conserved dsRNA-binding domains (DRBD) of approximately 65-68 amino acids, are found in both eukaryotes and prokaryotes and are even encoded by plants and viruses. DRBP's do not recognize specific nucleotide sequences and primarily interact with approximately 11-16 base pairs present within A-form double helix RNAs, which can include ssRNA's with extensive secondary structure. The DRBP family include TRBP ((T) under bar AR (R) under bar NA binding protein), PKR (protein kinase activated by ds (R) under bar NA), PACT (Protein Activator of PKR), ADAR (Adenosine deaminases acting on (R) under bar NA), and the RNase III family including DICER, which collectively play important roles in mRNA elongation, RNA interference (RNAi), mRNA editing, stability, splicing and/or export and translation. Here, we focus on the role of DRBP's referred to as the NFARs (Nuclear Factors associated with dsRNA) which are translated from two major alternatively spliced products encoded from a single gene. Evidence indicates that the NFAR proteins play crucial roles in mRNA post-transcriptional regulation, including mRNA stability, export and translation and may also have an important function in host defense.
引用
收藏
页码:35 / 39
页数:5
相关论文
共 57 条
[11]  
CORTHESY B, 1994, J BIOL CHEM, V269, P20682
[12]   Nuclear mRNA export: insights from virology [J].
Cullen, BR .
TRENDS IN BIOCHEMICAL SCIENCES, 2003, 28 (08) :419-424
[13]   Nuclear export of mRNA: from the site of transcription to the cytoplasm [J].
Erkmann, JA ;
Kutay, U .
EXPERIMENTAL CELL RESEARCH, 2004, 296 (01) :12-20
[14]   Proteins binding to duplexed RNA: one motif, multiple functions [J].
Fierro-Monti, I ;
Mathews, MB .
TRENDS IN BIOCHEMICAL SCIENCES, 2000, 25 (05) :241-246
[15]   Viral interactions with the nuclear transport machinery: Discovering and disrupting pathways [J].
Fontoura, BMA ;
Faria, PA ;
Nussenzveig, DR .
IUBMB LIFE, 2005, 57 (02) :65-72
[16]   Minihelix-containing RNAs mediate exportin-5-dependent nuclear export of the double-stranded RNA-binding protein ILF3 [J].
Gwizdek, C ;
Ossareh-Nazari, B ;
Brownawell, AM ;
Evers, S ;
Macara, IG ;
Dargemont, C .
JOURNAL OF BIOLOGICAL CHEMISTRY, 2004, 279 (02) :884-891
[17]   Members of the NF90/NFAR protein group are involved in the life cycle of a positive-strand RNA virus [J].
Isken, O ;
Grassmann, CW ;
Sarisky, RT ;
Kann, M ;
Zhang, S ;
Grosse, F ;
Kao, PN ;
Behrens, SE .
EMBO JOURNAL, 2003, 22 (21) :5655-5665
[18]   Nuclear factors are involved in hepatitis C virus RNA replication [J].
Isken, Olaf ;
Baroth, Martina ;
Grassmann, Claus W. ;
Weinlich, Susan ;
Ostareck, Dirk H. ;
Ostareck-Lederer, Antje ;
Behrens, Sven-Erik .
RNA, 2007, 13 (10) :1675-1692
[19]   Tap and NXT promote translation of unspliced mRNA [J].
Jin, L ;
Guzik, BW ;
Bor, YC ;
Rekosh, D ;
Hammarskjöld, ML .
GENES & DEVELOPMENT, 2003, 17 (24) :3075-3086
[20]  
KAO PN, 1994, J BIOL CHEM, V269, P20691