Structural and functional insights into a dodecameric molecular machine – The RuvBL1/RuvBL2 complex

Gorynia, Sabine; Bandeiras, Tiago M.; Pinho, Filipa G.; McVey, Colin E.; Vonrhein, Clemens; Round, Adam; Svergun, Dmitri I.; Donner, Peter; Matías, Pedro M.; Carrondo, Maria Arménia

doi:10.1016/j.jsb.2011.09.001

Cited by 109 publications

(188 citation statements)

References 70 publications

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“…X-ray crystallography (23)(24)(25) and electron microscopy (EM) (26 -28) revealed that RuvBL1 and RuvBL2 are organized in three domains. Domain I (DI) and III (DIII) comprise the catalytic ATPase core, responsible for the oligomerization in homo-hexameric rings with a central channel.…”

Section: Yin Yang 1 (Yy1)mentioning

confidence: 99%

“…Domain I (DI) and III (DIII) comprise the catalytic ATPase core, responsible for the oligomerization in homo-hexameric rings with a central channel. RuvBL1 and RuvBL2 also assemble hetero-oligomers with alternating RuvBL1 and RuvBL2 subunits (23)(24)(25). DII is a unique insertion connected to the ATPase core, resembling an OB-fold, and recombinant DII domains of RuvBL1 interact with ssDNA, dsDNA, and ssRNA in vitro (23)(24)(25).…”

Section: Yin Yang 1 (Yy1)mentioning

confidence: 99%

“…RuvBL1 and RuvBL2 also assemble hetero-oligomers with alternating RuvBL1 and RuvBL2 subunits (23)(24)(25). DII is a unique insertion connected to the ATPase core, resembling an OB-fold, and recombinant DII domains of RuvBL1 interact with ssDNA, dsDNA, and ssRNA in vitro (23)(24)(25). Using cryo-EM we recently solved the structure of human RuvBL1-RuvBL2 complexes assembled as hetero-dodecamers composed of two hexameric rings interacting back-to-back (27).…”

Section: Yin Yang 1 (Yy1)mentioning

confidence: 99%

“…RuvBL1 and RuvBL2 assemble homohexameric rings on their own, whereas its co-expression results in a mixture of hetero-hexameric and dodecameric complexes that are believed to be functional forms of these ATPases in the cell (23)(24)(25). We purified His-RuvBL1, His-RuvBL2, and HisRuvBL1-RuvBL2 complexes and also RuvBL1-RuvBL2 where the tag was removed (27) (Fig.…”

Section: Yy1 Multimerizes By the Association Of Dimers-mentioning

confidence: 99%

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Structure of Yin Yang 1 Oligomers That Cooperate with RuvBL1-RuvBL2 ATPases

López-Perrote

Alatwi

Torreira

et al. 2014

Journal of Biological Chemistry

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Background: Oligomerization of transcription factor YY1 is not well understood. Results: YY1 assembles homo-oligomers that bind DNAs without the consensus sequence, whose structure is studied by electron microscopy. Conclusion: RuvBL1-RuvBL2 enhances YY1 binding to DNAs without the consensus sequence for the transcription factor. Significance: YY1-RuvBL1-RuvBL2 complexes could contribute to functions beyond transcription, and we find this occurs during homologous recombination.

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Section: Yin Yang 1 (Yy1)mentioning

confidence: 99%

Section: Yin Yang 1 (Yy1)mentioning

confidence: 99%

Section: Yin Yang 1 (Yy1)mentioning

confidence: 99%

Section: Yy1 Multimerizes By the Association Of Dimers-mentioning

confidence: 99%

See 2 more Smart Citations

Structure of Yin Yang 1 Oligomers That Cooperate with RuvBL1-RuvBL2 ATPases

López-Perrote

Alatwi

Torreira

et al. 2014

Journal of Biological Chemistry

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“…However, we show here that cells reconstituted with the Reptin Walker B mutants expressed normal levels of Pontin such as those reconstituted with WT siRNA-resistant Reptin (20), thus ruling out that some of the effects seen with the mutants might be due to the loss of Pontin. Although the issue is not completely settled, the most recent evidence suggests that human Reptin and Pontin are organized in heterohexamers (24)(25)(26). It is thus likely that, when expressed in the presence of endogenous Reptin and Pontin, Walker B mutants will replace WT Reptin within hexamers and can thus exert a dominant negative effect.…”

Section: Discussionmentioning

confidence: 99%

The ATPase Activity of Reptin Is Required for Its Effects on Tumor Cell Growth and Viability in Hepatocellular Carcinoma

Grigoletto

Neaud

Allain-Courtois

et al. 2013

Molecular Cancer Research

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Reptin is overexpressed in most human hepatocellular carcinomas. Reptin is involved in chromatin remodeling, transcription regulation, or supramolecular complexes assembly. Its silencing leads to growth arrest and apoptosis in cultured hepatocellular carcinoma cells and stops hepatocellular carcinoma progression in xenografts. Reptin has an ATPase activity linked to Walker A and B domains. It is unclear whether every Reptin function depends on its ATPase activity. Here, we expressed Walker B ATPase-dead mutants (D299N or E300G) in hepatocellular carcinoma cells in the presence of endogenous Reptin. Then, we silenced endogenous Reptin and substituted it with siRNA-resistant wild-type (WT) or Flag-Reptin mutants. There was a significant decrease in cell growth when expressing either mutant in the presence of endogenous Reptin, revealing a dominant negative effect of the ATPase dead mutants on hepatocellular carcinoma cell growth. Substitution of endogenous Reptin by WT Flag-Reptin rescued cell growth of HuH7. On the other hand, substitution by Flag-Reptin D299N or E300G led to cell growth arrest. Similar results were seen with Hep3B cells. Reptin silencing in HuH7 cells led to an increased apoptotic cell death, which was prevented by WT Flag-Reptin but not by the D299N mutant. These data show that Reptin functions relevant for cancer are dependent on its ATPase activity, and suggest that antagonists of Reptin

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The gamma‐tubulin ring complex: Deciphering the molecular organization and assembly mechanism of a major vertebrate microtubule nucleator

et al. 2021

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Microtubules are protein cylinders with functions in cell motility, signal sensing, cell organization, intracellular transport, and chromosome segregation. One of the key properties of microtubules is their dynamic architecture, allowing them to grow and shrink in length by adding or removing copies of their basic subunit, the heterodimer αβ-tubulin. In higher eukaryotes, de novo assembly of microtubules from αβ-tubulin is initiated by a 2 MDa multi-subunit complex, the gamma-tubulin ring complex (γ-TuRC). For many years, the structure of the γ-TuRC and the function of its subunits remained enigmatic, although structural data from the much simpler yeast counterpart, the γ-tubulin small complex (γ-TuSC), were available. Two recent breakthroughs in the field, high-resolution structural analysis and recombinant reconstitution of the complex, have revolutionized our knowledge about the architecture and function of the γ-TuRC and will form the basis for addressing outstanding questions about biogenesis and regulation of this essential microtubule organizer. K E Y W O R D Sgamma-tubulin ring complex, gamma-tubulin small complex, gamma-tubulin, microtubule nucleation, microtubules, recombinant gamma-tubulin ring complex Abbreviations: AAA+, adenosine triphosphatases associated with various cellular activities;Arps, actin-related proteins; CDK5RAP2, CDK5 regulatory subunit-associated protein 2; CEP192, centrosomal protein of 192 kDa; ch-TOG, colonic hepatic tumor-overexpressed gene; CM1, centrosomin motif 1; GCP, γ-TuC component protein; γ-TuCs, γ-tubulin complexes; γ-TuRC, γ-tubulin ring complex; γ-TuSC, γ-tubulin small complex; GRIP1/2, γ-tubulin ring protein 1/2; HSP90, heat shock protein 90; INO80, inositol-requiring mutant 80 complex; MZT1/2, mitotic spindle organizing protein 1/2; NEDD1, neural precursor cell expressed, developmentally down-regulated 1; NME7, nucleotide diphosphate kinase 7; PCM, pericentriolar material; PIH1D1, PIH1 domain containing 1; R2TP, Rvb1-Rvb2-Tah1-Pih1; RPAP3, RNA polymerase II associated protein 3; RUVBL1/2, RuvB-like 1/2; SPB, spindle pole body; SWR1, SWI2/SNF2-related 1 complex; XMAP215, Xenopus microtubule assembly protein with 215 kDThis is an open access article under the terms of the Creative Commons Attribution License, which permits use, distribution and reproduction in any medium, provided the original work is properly cited.

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Structural and functional insights into a dodecameric molecular machine – The RuvBL1/RuvBL2 complex

Cited by 109 publications

References 70 publications

Structure of Yin Yang 1 Oligomers That Cooperate with RuvBL1-RuvBL2 ATPases

Structure of Yin Yang 1 Oligomers That Cooperate with RuvBL1-RuvBL2 ATPases

The ATPase Activity of Reptin Is Required for Its Effects on Tumor Cell Growth and Viability in Hepatocellular Carcinoma

The gamma‐tubulin ring complex: Deciphering the molecular organization and assembly mechanism of a major vertebrate microtubule nucleator

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