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The enzymes and control of eukaryotic mRNA turnover
TLDR
It is highlighted that there are a variety of enzymes with different specificities, suggesting that individual nucleases act on distinct subpopulations of transcripts within the cell and multiple mechanisms by which mRNA degradation could be regulated.
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The Crystal Structure of Human Eukaryotic Release Factor eRF1—Mechanism of Stop Codon Recognition and Peptidyl-tRNA Hydrolysis
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Decapping activators in Saccharomyces cerevisiae act by multiple mechanisms.
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Structural basis of dcp2 recognition and activation by dcp1.
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Structural basis of YAP recognition by TEAD4 in the hippo pathway.
TLDR
The crystal structure of the YAP-interacting C-terminal domain of TEAD4 in complex with the TEAD-interacted N-terminals of YAP is described and Mutagenesis reveals that the PXXPhiP motif of Yap, although making few contacts with TEad4, is important for TEAD 4 interaction as well as for the transforming activity.
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Structural and functional similarity between the Vgll1-TEAD and the YAP-TEAD complexes.
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RF3 Induces Ribosomal Conformational Changes Responsible for Dissociation of Class I Release Factors
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Structural basis for recruitment of RILP by small GTPase Rab7
TLDR
Structural comparison suggests that the combined use of RabSF1 and RabSF4 with the switch regions may be a general mode of action for most Rab proteins in regulating membrane trafficking.
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Structural insight into poly(A) binding and catalytic mechanism of human PARN
TLDR
The crystal structure of C‐terminal truncated human PARN determined in two states reveals that PARNn is folded into two domains, an R3H domain and a nuclease domain similar to those of Pop2p and ε186.
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Structural insights into eRF3 and stop codon recognition by eRF1.
TLDR
The crystal structures of human and Schizosaccharomyces pombe full-length eRF1 in complex with eRF3 lacking the GTPase domain revealed details of the interaction between these two factors and marked conformational changes in e RF1 that occur upon binding to e RF3, leading eRF 1 to resemble a tRNA molecule.
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