2014
DOI: 10.1083/jcb.201404160
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Proteomic and 3D structure analyses highlight the C/D box snoRNP assembly mechanism and its control

Abstract: During small nucleolar ribonucleoprotein complex assembly, a pre-snoRNP complex consisting only of protein components forms first, followed by displacement of the ZNHIT3 subunit when C/D snoRNAs bind and dynamic loading and unloading of RuvBL AAA+ ATPases.

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Cited by 63 publications
(157 citation statements)
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“…As mentioned previously, ZNHIT6 and ZNHIT3 are snoRNP biogenesis factors that interact with NUFIP1 and the AAA+ ATPases91415. ZNHIT1 and INO80B/ZNHIT4 are components of chromatin remodelling complexes SRCAP and INO80, respectively, both of which also harbour a RUVBL1 and RUVBL2 module7.…”
Section: Resultsmentioning
confidence: 88%
“…As mentioned previously, ZNHIT6 and ZNHIT3 are snoRNP biogenesis factors that interact with NUFIP1 and the AAA+ ATPases91415. ZNHIT1 and INO80B/ZNHIT4 are components of chromatin remodelling complexes SRCAP and INO80, respectively, both of which also harbour a RUVBL1 and RUVBL2 module7.…”
Section: Resultsmentioning
confidence: 88%
“…Our affinity purification/mass spectrometry analyses confirmed the interaction of ECD with PRPF8. The R2TP complex regulates mRNA and ribosome biogenesis by facilitating the assembly of small nucleolar ribonucleoproteins (snoRNPs), which are known to be involved in spliceosome modification (51,52). Upregulation of R2TP and snoRNP components is thought to promote ribosome synthesis in cancer cells (47).…”
Section: Discussionmentioning
confidence: 99%
“…Interestingly, only ATP-loaded RUVBL1/2 can bind to ZNHIT6, whereas the binding of ATP releases RUVBL1/2 from R2TP 69,89 . This would suggest that it is the ATP loaded form of RUVBL1/2 that binds the pre-snoRNP complex and that the role of the HSP90/R2TP system would thus be to liberate RUVBL1/2 from R2TP to load them on the core proteins SNU13 and NOP58 84 . In agreement with this idea, yeast NOP58 mutants that fail to assemble with SNU13 interact more strongly with yeast R2TP and in particular with the yeast homologs of PIH1D1 and RPAP3 78 …”
Section: Introductionmentioning
confidence: 99%
“…In higher eukaryotes, NOP58 lacks the DSDD motif. These organisms however have the C12orf45 factor, which tighly associates with NOP58 and may mediate its interaction with the R2TP 84 . Thus, the details of interactions might differ substantially between yeast and human systems, in agreement with rather important differences between the homologs of PIH1D1 and RPAP3.…”
Section: Introductionmentioning
confidence: 99%