p72: a human nuclear DEAD box protein highly related to p68

Lamm, Gâbor M.; Nicol, Samantha M.; Fuller-Pace, Frances V.; Lamond, Angus I.

doi:10.1093/nar/24.19.3739

Cited by 94 publications

(92 citation statements)

References 55 publications

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“…Expression of a p72 mRNA containing introns 9 or 11 would lead to polypeptides of 363 and 407 amino acids, respectively, which were not detected in HeLa cells (see below). Two p72 RNA species of about 5 and 9 kb had also been found previously in Northern blot analyses of human tissues (12) and vertebrate cell lines (13) in variable amounts and ratios.…”

Section: Resultssupporting

confidence: 73%

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The mRNA of DEAD Box Protein p72 Is Alternatively Translated into an 82-kDa RNA Helicase

Uhlmann‐Schiffler

Rößler

Stahl

2002

Journal of Biological Chemistry

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p68 and p72 are two highly related DEAD box proteins with similar biochemical activities in the nucleus of vertebrate cells; it is unknown whether they have redundant or differential in vivo functions. We report on a third member of this subfamily that is alternatively expressed from p72 mRNA. A detailed analysis of HeLa p72 mRNA was performed. It has an overall length of more than 5 kb and contains a 0.75-kb 5-untranslated region and a 3-untranslated region of 2.5 kb. Its open reading frame extends to nucleotide ؊243 upstream of the first in-frame AUG (A in the AUG triplet is ؉1) which serves as the p72 translation initiator codon. We provide evidence that alternative translation at a non-AUG within the extra coding region of this mRNA yields an 82-kDa protein (p82). Immunological studies substantiate that p82 is a naturally existing p72 variant and that both proteins are expressed at similar concentrations. p82 purified from HeLa cells is an ATP-dependent RNA helicase with biochemical properties almost identical to those of p72.Control of transcription is generally considered the main regulation level of mammalian gene expression, although mRNA maturation and modulation of mRNA stability or translational efficiency also contribute to expression control (1). Generation of protein variants by alternative pre-mRNA splicing or alternative initiation of mRNA translation enlarges the coding capacity and may explain the relatively low number of genes actually found in the human genome. According to recent estimations, on average one gene encodes three proteins (2).Although the 5Ј-untranslated leader sequences (UTRs) 1 of most vertebrate mRNAs are less than 100 nucleotides (nt) long (3), those of tightly controlled genes usually are longer and are GC-rich. Such structure-prone 5Ј-UTRs can modulate translation by the presence of upstream (up) open reading frames (ORFs) in addition to the main ORF, by formation of secondary structures, and/or by RNA-protein interactions (4). Indeed, they appear particularly characteristic of mRNAs encoding growth factors, receptor proteins, transcription factors, signal transduction components, proto-oncogenes, tumor suppressor proteins, and even proteins that mostly are constitutively expressed at a low level ("housekeeping" proteins).DEAD/DEXH box proteins belonging to superfamily II of RNA helicases play a universal role in RNA metabolism of proand eukaryotes. Not surprisingly, they are involved in gene expression control, for instance during germ cell and embryonic development or in cell proliferation and differentiation (5). This in turn requires tight control of at least some DEAD/DEXH box proteins like CsdA of Escherichia coli, which is regulated by an 11-nt "cold box" sequence in its 5Ј-UTR (6), or the Saccharomyces cerevisiae Dbp2, the gene of which contains an unusually large intron that is part of a post-transcriptional autoregulatory feedback loop (7). A similarly complex transcription regulation has been shown for nuclear p68 (8), a mammalian homologue of Dbp2. In addition,...

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Section: Resultssupporting

confidence: 73%

“…p72, another human DEAD box protein (12), is highly homologous to p68. It is, like p68, transcribed in a tissue-specific manner and seems to be involved in neuronal differentiation (13).…”

mentioning

confidence: 99%

The mRNA of DEAD Box Protein p72 Is Alternatively Translated into an 82-kDa RNA Helicase

Uhlmann‐Schiffler

Rößler

Stahl

2002

Journal of Biological Chemistry

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“…Thus, it is tempting to speculate that the presence of p68 in keratinocyte nuclei might be associated to a distinct phase of the cell cycle. Consistently, p68 has been described to localize in the nuclei of interphase cells in vitro (39,40), an observation that supports the presence of high numbers of p68 negative cells in normal wound tissue, as the neo-epithelium is largely characterized by mitogenic cells (17). Evidently, the localization of p68 in interphase cells might provide the explanation for elevated p68 levels observed in NO-deficient healing.…”

Section: Identification Of P68 As a Novel No-regulated Gene In Kera-supporting

confidence: 57%

p68 DEAD Box RNA Helicase Expression in Keratinocytes

Kahlina

Goren

Pfeilschifter

et al. 2004

Journal of Biological Chemistry

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“…During interphase, P68 is found in the nucleoplasm and excluded from the nucleoli. The granular pattern of P68 distribution is well documented (Lane and Hoeffer, 1980;Lamm et al, 1996;Nicol et al, 2000).…”

Section: Intranuclear Localisation Of P68mentioning

confidence: 92%

Satellite DNA binding and cellular localisation of RNA helicase P68

Enukashvily

Donev

Sheer

et al. 2005

Journal of Cell Science

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We purified a 68-kDa protein from the mouse nuclear matrix using ion exchange and affinity chromatography. Column fractions were tested for specific binding to mouse minor satellite DNA using a gel mobility shift assay. The protein was identified by mass spectrometry as RNA helicase P68. In fixed cells, P68 was found to shuttle in and out of SC35 domains, forming fibres and granules in a cell-cycle dependent manner. Analysis of the P68 sequence revealed a short potential coiled-coil domain that might be involved in the formation of P68 fibres. Contacts between centromeres and P68 granules were observed during all phases of the cycle but they were most prominent in mitosis. At this stage, P68 was found in both the centromeric regions and the connections between chromosomes. Direct interaction of P68/DEAD box RNA helicase with satellite DNAs in vitro has not been demonstrated for any other members of the RNA helicase family.

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p72: a human nuclear DEAD box protein highly related to p68

Cited by 94 publications

References 55 publications

The mRNA of DEAD Box Protein p72 Is Alternatively Translated into an 82-kDa RNA Helicase

The mRNA of DEAD Box Protein p72 Is Alternatively Translated into an 82-kDa RNA Helicase

p68 DEAD Box RNA Helicase Expression in Keratinocytes

Satellite DNA binding and cellular localisation of RNA helicase P68

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