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J. Biol. Chem., Vol. 276, Issue 25, 23144-23154, June 22, 2001
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From the Office of Clinical Research and Laboratory of Signal
Transduction, NIEHS, National Institutes of Health, Research Triangle
Park, North Carolina 27709 and the Departments of Medicine and
Biochemistry, Duke University Medical Center,
Durham, North Carolina 27710
The CCCH family of tandem zinc finger proteins
has recently been shown to promote the turnover of certain mRNAs
containing class II AU-rich elements (AREs). In the case of one member
of this family, tristetraprolin (TTP), absence of the protein in knockout mice leads to stabilization of two mRNAs containing AREs of this type, those encoding tumor necrosis factor
Interactions of CCCH Zinc Finger Proteins with mRNA
TRISTETRAPROLIN-MEDIATED AU-RICH ELEMENT-DEPENDENT mRNA
DEGRADATION CAN OCCUR IN THE ABSENCE OF A POLY(A) TAIL*
(TNF) and granulocyte-macrophage colony-stimulating factor. To begin to decipher the mechanism by which these zinc finger proteins stimulate the breakdown of this class of mRNAs, we co-transfected TTP and its
related CCCH proteins into 293 cells with vectors encoding full-length
TNF, granulocyte-macrophage colony-stimulating factor, and
interleukin-3 mRNAs. Co-expression of the CCCH proteins caused the
rapid turnover of these ARE-containing mRNAs and also promoted the
accumulation of stable breakdown intermediates that were truncated at
the 3'-end of the mRNA, even further 5' than the 5'-end of the
poly(A) tail. To determine whether an intact poly(A) tail was necessary
for TTP to promote this type of mRNA degradation, we inserted the
TNF ARE into a nonpolyadenylated histone mRNA and also attached
a histone 3'-end-processing sequence to the 3'-end of nonpolyadenylated
interleukin-3 and TNF mRNAs. In all three cases, TTP stimulated
the turnover of the ARE-containing mRNAs, despite the demonstrated
absence of a poly(A) tail. These studies indicate that members of this
class of CCCH proteins can promote class II ARE-containing mRNA
turnover even in the absence of a poly(A) tail, suggesting that the
processive removal of the poly(A) tail may not be required for this
type of CCCH protein-stimulated mRNA turnover.
*
This work was supported in part by a Cooperative Research
and Development Agreement with AstraZeneca Pharmaceuticals, PLC.The costs of publication of this
article were defrayed in part by the
payment of page charges. The article
must therefore be hereby marked
"advertisement" in
accordance with 18 U.S.C. Section
1734 solely to indicate this fact.
To whom correspondence should be addressed: A2-05 NIEHS, 111 Alexander Dr., Research Triangle Park, NC 27709. Tel.: 919-541-4899; Fax: 919-541-4571; E-mail: black009@niehs.nih.gov.
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