Abstract：
:TIAR and HuR are mRNA-binding proteins that play important roles in the regulation of translation. They both possess three RNA recognition motifs (RRMs) and bind to AU-rich elements (AREs), with seemingly overlapping specificity. Here we show using SPR that TIAR and HuR bind to both U-rich and AU-rich RNA in the nanomolar range, with higher overall affinity for U-rich RNA. However, the higher affinity for U-rich sequences is mainly due to faster association with U-rich RNA, which we propose is a reflection of the higher probability of association. Differences between TIAR and HuR are observed in their modes of binding to RNA. TIAR is able to bind deoxy-oligonucleotides with nanomolar affinity, whereas HuR affinity is reduced to a micromolar level. Studies with U-rich DNA reveal that TIAR binding depends less on the 2'-hydroxyl group of RNA than HuR binding. Finally we show that SAXS data, recorded for the first two domains of TIAR in complex with RNA, are more consistent with a flexible, elongated shape and not the compact shape that the first two domains of Hu proteins adopt upon binding to RNA. We thus propose that these triple-RRM proteins, which compete for the same binding sites in cells, interact with their targets in fundamentally different ways.
journal_name
Nucleic Acids Resjournal_title
Nucleic acids researchauthors
Kim HS,Wilce MC,Yoga YM,Pendini NR,Gunzburg MJ,Cowieson NP,Wilson GM,Williams BR,Gorospe M,Wilce JAdoi
10.1093/nar/gkq837subject
Has Abstractpub_date
2011-02-01 00:00:00pages
1117-30issue
3eissn
0305-1048issn
1362-4962pii
gkq837journal_volume
39pub_type
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journal_title：Nucleic acids research
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pub_type： 杂志文章
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更新日期：1983-11-11 00:00:00
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pub_type： 杂志文章
doi：10.1093/nar/13.8.2931
更新日期：1985-04-25 00:00:00
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journal_title：Nucleic acids research
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doi：10.1093/nar/gkl773
更新日期：2006-01-01 00:00:00
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