Abstract
A + U-rich elements (ARE) serve to control the degradation of some proto-oncogene and lymphokine mRNAs. The protein, AUF1, which consists of two polypeptides of 37 and 40 kDa (p37 and p40, respectively) when purified from cytosol, has been implicated in ARE-directed mRNA turnover due to its binding to ARE. Molecular cloning of a cDNA (p37AUF1) corresponding to human p37 predicted a polypeptide containing two non-identical RNA recognition motifs (RRM) and a C-terminal Gin-rich domain [Zhang et al. Mol. Cell. Biol. 13 (1993) 7652-7665]. Two cDNAs, designated mu AUF1-3 and muAUF1-7, were isolated from a murine fetal cDNA library, using as a probe, a fragment of the p37AUF1 cDNA encoding RRM1 and approximately half of RRM2. The muAUFl-3 open reading frame (ORF) was very homologous to human p37AVF1 with the greatest homology between the corresponding RRMs and the C-terminal Gin-rich motif. Clone muAUFl-7 was highly homologous to muAUFl-3, but was truncated within the region encoding the RNP-1 box in RRM2. Clone muAUFl-3 encoded 19 amino acids in RRM1 not encoded by either muAUFl-7 or human p37AUF1. Such alterations in sequence could modify the RNA-binding properties of these proteins and have concomitant effects on ARE-directed posttranscriptional processes.
Original language | English (US) |
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Pages (from-to) | 315-319 |
Number of pages | 5 |
Journal | Gene |
Volume | 149 |
Issue number | 2 |
DOIs | |
State | Published - Nov 18 1994 |
Externally published | Yes |
Keywords
- cytokine
- degradation
- mRNA stability
- proto-oncogene
ASJC Scopus subject areas
- Genetics