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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
Related Articles

Impaired binding of standard initiation factors eIF3b, eIF4G and eIF4B to domain V of the live-attenuated coxsackievirus B3 Sabin3-like IRES--alternatives for 5'UTR-related cardiovirulence mechanisms.

Diagn Pathol. 2013;8:161

Authors: Souii A, Gharbi J, Ben M'hadheb-Gharbi M

Abstract
UNLABELLED: Internal ribosome entry site (IRES) elements fold into highly organized conserved secondary and probably tertiary structures that guide the ribosome to an internal site of the RNA at the IRES 3'end. The composition of the cellular proteome is under the control of multiple processes, one of the most important being translation initiation. In each poliovirus Sabin vaccine strain, a single point mutation in the IRES secondary-structure domain V is a major determinant of neurovirulence and translation attenuation. Here we are extrapolating poliovirus findings to a genomic related virus named coxsackievirus B3 CVB3); a causative agent of viral myocarditis. We have previously reported that Sabin3-like mutation (U473 → C) introduced in the domain V sequence of the CVB3 IRES led to a defective mutant with a serious reduction in translation efficiency and ribosomal initiation complex assembly, besides an impaired RNA-protein binding pattern. With the aim to identify proteins interacting with both CVB3 wild-type and Sabin3-like domain V RNAs and to assess the effect of the Sabin3-like mutation on these potential interactions, we have used a proteomic approach. This procedure allowed the identification of three RNA-binding proteins interacting with the domain V: eIF4G (p220), eIF3b (p116) and eIF4B (p80). Moreover, we report that this single-nucleotide exchange impairs the interaction pattern and the binding affinity of these standard translation initiation factors within the IRES domain V of the mutant strain. Taken together, these data indicate how this decisive Sabin3-like mutation mediates viral translation attenuation; playing a key role in the understanding of the cardiovirulence attenuation within this construct. Hence, these data provide further evidence for the crucial role of RNA structure for the IRES activity, and reinforce the idea of a distribution of function between the different IRES structural domains.
VIRTUAL SLIDE: The virtual slide(s) for this article can be found here: http://www.diagnosticpathology.diagnomx.eu/vs/6160165131045880.

PMID: 24063684 [PubMed - indexed for MEDLINE]

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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