 |
PDBsum entry 5eim
|
|
|
|
 |
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
 |
|
|
|
 |
 |
 |
 |
 |
 |
 |
 |
 |
 |
 |
 |
 |
 |
 |
 |
 |
 |
|
|
|
|
|
|
|
|
|
|
RNA binding protein/RNA
|
PDB id
|
|
|
|
5eim
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
References listed in PDB file
|
 |
|
Key reference
|
 |
|
Title
|
 |
Structural insights into the specific recognition of dsr by the yth domain containing protein mmi1.
|
 |
|
Authors
|
 |
B.Wu,
J.Xu,
S.Su,
H.Liu,
J.Gan,
J.Ma.
|
 |
|
Ref.
|
 |
Biochem Biophys Res Commun, 2017,
491,
310-316.
[DOI no: ]
|
 |
|
PubMed id
|
 |
|
 |
|
|
 |
 |
|
Abstract
|
 |
|
Meiosis is one of the most dramatic differentiation programs accompanied by a
striking change in gene expression profiles in fission yeast Schizosaccharomyces
pombe. Whereas a number of meiosis-specific transcripts are expressed untimely
in mitotic cells, and the entry of meiosis will be blocked as the accumulation
of meiosis-specific mRNAs in the mitotic cells. A YTH domain containing protein
Mmi1 was identified as a pivotal effector in a post-transcriptional event termed
selective elimination of meiosis-specific mRNAs. Mmi1 can recognize and bind a
class of meiosis-specific transcripts expressed inappropriately in mitotic
cells, which all contain a conservative region called DSR, as a mark to remove
them in cooperation with nuclear exosomes. Here we report the 1.6 Å resolution
crystal structure of the Mmi1-YTH domain in complex with a high consensus
hexanucleotide motif, which is multiple copied in the DSR region. Our structure
observations, supported by site-directed mutations of key residues illustrate
the mechanism for specific recognition of DSR-RNA by Mmi1. Moreover, different
from other YTH domain family proteins, Mmi1-YTH domain has a distinctive
RNA-binding properties although it has a similar fold as other ones.
|
 |
|
|
|
|
 |