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Welcome to ZOMEBase, the information center for the three PCI Zomes: COP9 Signalosome, the regulatory lid of the 26S proteasome and eIF3

What is a ZOME?

A "ZOME" is any one of three related multi-protein complexes:

the Cop9 Signalosome
the Regulatory Lid of the 26S proteasome
eIF3

These complexes were grouped together on the basis of similarities in their subunit composition and predicted structure. While subunits between the complexes share little primary sequence similarity, six subunits of all three complexes contain a PCI (Proteasome, CSN, eIF3) motif, while two subunits carry an MPN (Mpr1, Pad1, N-terminal) motif. This conserved six PCI / two MPN structure (among most higher eukaryotes) strongly suggests a common ancestor for these complexes. (1)

ZOMES, individually and in concert, affect proteome composition.

In ZOMEBase you can find

Want to contribute to ZOMEBase?

All Zomers are welcome and invited to contribute to and modify ZOMEBase using the Twiki editor on each page. To edit, you'll need a username and password. Please contact dannyc@tauex.tau.ac.il . As a contributer you can edit and add to exisiting content including making new pages.

Pages that need to be worked on

ZOMEBase Utilities

Recent ZOMES articles

NCBI: db=pubmed; Term=cop9 or "proteasome lid" or eIF3 or jab1

The Not5 Subunit of the Ccr4-Not Complex Connects Transcription and Translation.

PLoS Genet. 2014 Oct;10(10):e1004569

Authors: Villanyi Z, Ribaud V, Kassem S, Panasenko OO, Pahi Z, Gupta I, Steinmetz L, Boros I, Collart MA

Abstract
Recent studies have suggested that a sub-complex of RNA polymerase II composed of Rpb4 and Rpb7 couples the nuclear and cytoplasmic stages of gene expression by associating with newly made mRNAs in the nucleus, and contributing to their translation and degradation in the cytoplasm. Here we show by yeast two hybrid and co-immunoprecipitation experiments, followed by ribosome fractionation and fluorescent microscopy, that a subunit of the Ccr4-Not complex, Not5, is essential in the nucleus for the cytoplasmic functions of Rpb4. Not5 interacts with Rpb4; it is required for the presence of Rpb4 in polysomes, for interaction of Rpb4 with the translation initiation factor eIF3 and for association of Rpb4 with mRNAs. We find that Rpb7 presence in the cytoplasm and polysomes is much less significant than that of Rpb4, and that it does not depend upon Not5. Hence Not5-dependence unlinks the cytoplasmic functions of Rpb4 and Rpb7. We additionally determine with RNA immunoprecipitation and native gel analysis that Not5 is needed in the cytoplasm for the co-translational assembly of RNA polymerase II. This stems from the importance of Not5 for the association of the R2TP Hsp90 co-chaperone with polysomes translating RPB1 mRNA to protect newly synthesized Rpb1 from aggregation. Hence taken together our results show that Not5 interconnects translation and transcription.

PMID: 25340856 [PubMed - as supplied by publisher]

Notes

1 : Hofmann, K., and Bucher, P. (1998). The pci domain: A common theme in three multi-protein complexes. Trends Biochem Sci 23, 204-205.;Aravind, L., and Ponting, C.P. (1998). Homologues of 26S proteasome subunits are regulators of transcription and translation. Protein Sci 7, 1250-1254.; Kim, T.-H., Hofmann, K., von Arnim, A.G., and Chamovitz, D.A. (2001). The pci complexes:pretty complex interations in diverse signaling pathways. Trend Plant Sciences 6, 379-386.


r21 - 02 Aug 2010 - 12:15:05 - IdoGan
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