Abstract:
:The tandem zinc finger (TZF) domain of the protein TIS11d binds to the class II AU-rich element (ARE) in the 3' untranslated region (3' UTR) of target mRNAs and promotes their deadenylation and degradation. The NMR structure of the TIS11d TZF domain bound to the RNA sequence 5'-UUAUUUAUU-3' comprises a pair of novel CCCH fingers of type CX(8)CX(5)CX(3)H separated by an 18-residue linker. The two TIS11d zinc fingers bind in a symmetrical fashion to adjacent 5'-UAUU-3' subsites on the single-stranded RNA via a combination of electrostatic and hydrogen-bonding interactions, with intercalative stacking between conserved aromatic side chains and the RNA bases. Sequence specificity in RNA recognition is achieved by a network of intermolecular hydrogen bonds, mostly between TIS11d main-chain functional groups and the Watson-Crick edges of the bases. The TIS11d structure provides insights into the RNA-binding functions of this large family of CCCH zinc finger proteins.
journal_name
Nat Struct Mol Bioljournal_title
Nature structural & molecular biologyauthors
Hudson BP,Martinez-Yamout MA,Dyson HJ,Wright PEdoi
10.1038/nsmb738keywords:
subject
Has Abstractpub_date
2004-03-01 00:00:00pages
257-64issue
3eissn
1545-9993issn
1545-9985pii
nsmb738journal_volume
11pub_type
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