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Schlagwörter:
BOX PROTEIN DHH1P; CRYSTAL-STRUCTURE; STRUCTURAL BASIS; SACCHAROMYCES-CEREVISIAE; CCR4-NOT COMPLEX; ENZYME DCP2; TRANSLATIONAL REPRESSION; CAP RECOGNITION; NUDIX HYDROLASE; BINDING
Zusammenfassung:
Cellular mRNA levels are regulated via rates of transcription and decay. Since the removal of the mRNA 5'-cap by the decapping enzyme DCP2 is generally an irreversible step towards decay, it requires regulation. Control of DCP2 activity is likely effected by two interdependent means: by conformational control of the DCP2-DCP1 complex, and by assembly control of the decapping network, an array of mutually interacting effector proteins. Here, we compare three recent and conformationally distinct crystal structures of the DCP2-DCP1 decapping complex in the presence of substrate analogs and decapping enhancers and we discuss alternative substrate recognition modes for the catalytic domain of DCP2. Together with structure-based insight into decapping network assembly, we propose that DCP2-mediated decapping follows more than one path.
