Reptin and Pontin function antagonistically with PcG and TrxG complexes to mediate Hox gene control

Diop, Soda Balla; Bertaux, Karine; Dasari, Vasanthi; Sarkeshik, Ali; Goirand, Benjamin; Aragnol, Denise; Tolwinski, Nicholas S.; Cole, Michael; Pradel, Jacques; Yates, John R.; Mishra, Rakesh K.; Graba, Yacine; Saurin, Andrew J.

doi:10.1038/embor.2008.8

Cited by 53 publications

(53 citation statements)

References 25 publications

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“…Although RVB1 and RVB2 are complexed with each other in cells, there are several examples where the two proteins act independently of each other (43,44,45,46). The rescue of TIP60.com's HAT activity by either rRVB1 or rRVB2, however, suggests that the two proteins can also function alone and are redundant with each other.…”

Section: Discussionmentioning

confidence: 90%

RVBs Are Required for Assembling a Functional TIP60 Complex

Jha

Gupta

Dar

et al. 2013

Molecular and Cellular Biology

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RVB1/RVB2 (RuvBL1/RuvBL2 or pontin/reptin) are enigmatic AAA ؉ ATPase proteins that are present in multiple cellular complexes. Although they have been implicated in many cellular functions, the exact molecular function of RVB proteins in the various complexes is not clear. TIP60 complex (TIP60.com) is a tumor suppressor chromatin-remodeling complex containing RVB proteins. RVBs are required for the lysine acetyltransferase activity of TIP60.com but not for that of the pure recombinant TIP60 polypeptide. Here we describe two molecular functions of RVBs in TIP60.com. First, RVBs negate the repression of catalytic activity of TIP60 by another protein in TIP60.com, p400. RVBs competitively displace the SNF2 domain of p400 from the TIP60 polypeptide. In addition RVBs are also required for heat stability of TIP60.com by a p400-independent pathway. RVB1 and RVB2 are redundant with each other for these functions and do not require their ATPase activities. Thus, RVB proteins act as molecular adaptors that can substitute for one another to facilitate the optimal assembly, heat stability, and function of the TIP60 complex.

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Section: Discussionmentioning

confidence: 90%

RVBs Are Required for Assembling a Functional TIP60 Complex

Jha

Gupta

Dar

et al. 2013

Molecular and Cellular Biology

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“…The Uri complex probably contributes to the control of gene expression via the E3-ubiquitin ligase SCF Skp2 and its association with RNA polymerase II and the Paf complex (Adelman et al, 2006). Furthermore, Reptin in Drosophila is a component of the PRC1 complex (Qi et al, 2006), whereas Pontin purifies with the Brahma chromatin remodeling complex (Diop et al, 2008). Reporter gene assays demonstrated that Pontin and Reption antagonistically influence the transactivation potential of the ß-catenin-TCF complex, which is central to Wingless signaling (Bauer et al, 2000).…”

Section: The Myst Hat Dtip60 Is Part Of a Multiprotein Complexmentioning

confidence: 99%

Widespread regulation of gene expression in the Drosophila genome by the histone acetyltransferase dTip60

et al. 2009

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“…The cleared lysates were loaded onto a StrepTactin-Sepharose column (1-ml bed volume; IBA) by filtering through 0.45-m-pore-size polyethersulfone filter (Corning) and fractionated according to the manufacturer's instructions. The peak NS5A fraction from 30 preparations (12.5 g) was collected and concentrated by acetonemethanol precipitation and subjected to multidimensional protein identification technology (MudPIT) analysis (5,8,9,11,26,34,39,41). For the details of MudPIT analysis, see Materials and Methods in the supplemental material.…”

Section: Methodsmentioning

confidence: 99%

Role of Oxysterol Binding Protein in Hepatitis C Virus infection

Amako

Sarkeshik

Hotta

et al. 2009

J Virol

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118

126

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Hepatitis C virus (HCV) RNA genome replicates within the ribonucleoprotein (RNP) complex in the modified membranous structures extended from endoplasmic reticulum. A proteomic analysis of HCV RNP complexes revealed the association of oxysterol binding protein (OSBP) as one of the components of these complexes. OSBP interacted with the N-terminal domain I of the HCV NS5A protein and colocalized to the Golgi compartment with NS5A. An OSBP-specific short hairpin RNA that partially downregulated OSBP expression resulted in a decrease of the HCV particle release in culture supernatant with little effect on viral RNA replication. The pleckstrin homology (PH) domain located in the N-terminal region of OSBP targeted this protein to the Golgi apparatus. OSBP deletion mutation in the PH (⌬PH) domain failed to localize to the Golgi apparatus and inhibited the HCV particle release. These studies suggest a possible functional role of OSBP in the HCV maturation process.Hepatitis C virus (HCV) infection is one of the leading causes of chronic hepatitis. HCV infection is associated with cirrhosis, steatosis, and hepatocellular carcinoma (33). The HCV RNA genome of ϳ9.6 kb is translated via an internal ribosome entry site element on the rough endoplasmic reticulum (ER) as a polyprotein precursor of about 3,010 amino acids that is co-and posttranslationally processed by cellular and viral proteases into mature structural and nonstructural (NS) proteins (33). HCV replicates within ribonucleoprotein (RNP) complexes associated with modified ER membranous structures (15). Recent work implicated lipid droplets that emanate from the ER as sites of RNA replication (28,44). Almost all of the HCV NS proteins along with a variety of cellular factors are associated with the RNP complexes engaged in viral RNA replication (37). It is likely that these NS proteins not only participate in replication process but also are involved in the various steps of virion morphogenesis and assembly. Membrane-associated RNP complexes are generally composed of viral proteins, replicating RNA, host proteins, and altered cellular membranes (1). In this respect, a growing body of evidence implicates the functional role of NS5A in early steps of virion assembly and morphogenesis (3,27,45). NS5A is a phosphoprotein that migrates in sodium dodecyl sulfate gels as 56-kDa (basally phosphorylated) and 58-kDa (hyperphosphorylated) forms of proteins. The C-terminal domain III region of NS5A and the phosphorylated residue (Ser 457 ) are important for virion maturation (3, 27, 45). NS5A domain III contains the binding site for viral core protein, indicating the possible involvement of NS5A protein in virus assembly (27). NS5A anchors to the ER membrane by an N-terminal hydrophobic ␣-helix, and this attachment is needed for its key role(s) in viral replication (10). Studies suggest that phosphorylation of NS5A plays a functional role in viral replication (12). The hyperphosphorylated NS5A reduces its interaction with the human vesicle-associated membrane protein-associate...

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Reptin and Pontin function antagonistically with PcG and TrxG complexes to mediate Hox gene control

Cited by 53 publications

References 25 publications

RVBs Are Required for Assembling a Functional TIP60 Complex

RVBs Are Required for Assembling a Functional TIP60 Complex

Widespread regulation of gene expression in the Drosophila genome by the histone acetyltransferase dTip60

Role of Oxysterol Binding Protein in Hepatitis C Virus infection

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