Biochimica et Biophysica Acta (BBA) - Gene Structure and Expression
Short sequence-paperIsolation, molecular characterization, and tissue-specific expression of ECP-51 and ECP-54 (TIP49), two homologous, interacting erythroid cytosolic proteins1
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Plasmodium falciparum RuvB1 is an active DNA helicase and translocates in the 5'-3' direction
2013, GeneCitation Excerpt :While in another report human RuvBL1/TIP49a was present not only in the nucleus, as expected, but was also concentrated at the centrosome (Gartner et al., 2003). Some other studies also reported its partial (Boulon et al., 2008; Sigala et al., 2005) extra nuclear localization (Salzer et al., 1999). Thus on the basis of RuvB1 localization in P. falciparum it can be expected that it may be involved in the nuclear function.
Novel RuvB nuclear ATPase is specific to intraerythrocytic mitosis during schizogony of Plasmodium falciparum
2012, Molecular and Biochemical ParasitologyThe multifaceted proteins Reptin and Pontin as major players in cancer
2011, Biochimica et Biophysica Acta - Reviews on CancerCitation Excerpt :Quite to the contrary, when the same cells were grown in hypoxic conditions, Reptin silencing increased migration and invasion [35]. That Reptin and Pontin can have a cytosolic localization is clearly illustrated by their purification from the cytosol of erythrocytes, anuclear cells [40]. In addition, several publications have reported a partial cytoplasmic localization for Reptin in HeLa cells [5,46], HEK293 [111], adipocytes [129], and for Pontin in embryonic stem cells [39] and HeLa cells [5,7,130].
In vivo silencing of Reptin blocks the progression of human hepatocellular carcinoma in xenografts and is associated with replicative senescence
2010, Journal of HepatologyCitation Excerpt :Through a comparative study of the proteome of HCC with that of the peri-tumour liver, we identified the deregulation of a number of proteins [2], especially the overexpression of RuvBL2/Reptin [3]. Reptin is also known as TIP49b [4], TIP48 [5], Reptin52 [6], Rvb2 [7], TAP54β [8], and ECP-51 [9]. It belongs to the AAA + family of ATPases (reviewed in [10,11]) and shows a limited homology to the bacterial RuvB ATP-dependent DNA helicase.
RVB1/RVB2: Running Rings around Molecular Biology
2009, Molecular CellCitation Excerpt :RVB1 and RVB2 are ATP-binding proteins that belong to the AAA+ (ATPase associated with diverse cellular activities) family of ATPases. RVBs (RVB1 and RVB2) were discovered independently in multiple organisms (Bauer et al., 1998, 2000; Kanemaki et al., 1997, 1999; Qiu et al., 1998; Salzer et al., 1999; Wood et al., 2000) and implicated in many cellular pathways (Figure 1). The structure of the RVB1/RVB2 complex that has recently been elucidated suggests that RVBs could act as a scaffolding protein, explaining its appearance in diverse cellular protein complexes (Matias et al., 2006; Puri et al., 2007; Torreira et al., 2008).
- 1
The nucleotide sequence data reported in this paper will appear in the DDBJ, EMBL and GenBank databases with accession numbers Y18417 (ECP-51) and Y18418 (ECP-54).
- 2
These authors contributed equally to this study.