Identification of a novel human member of the DEAD box protein family

Suk, Kyoungho; Kim, Sunshin; Kim, Yun-Hee; Oh, Seung-Hoon; Lee, Moon‐Kyu; Kim, Kwang-Won; Kim, Hee-Dai; Seo, Yeon‐Soo; Lee, Myung-Shik

doi:10.1016/s0925-4439(00)00010-7

Cited by 6 publications

(5 citation statements)

References 21 publications

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“…Northern blotting with a ddx42-specific probe revealed an mRNA of ∼4 kb, which occurs in similar concentration in HeLa, Hep3B, COS, TC7 and HaCaT cells ( Figure 2B ). The coding sequence (cds) of the ddx42 mRNA was found by RT–PCR to be extended further 5′-ward than reported previously ( 41 , 49 ), resulting in a polypeptide consisting of 938 amino acids (compare Figure 2A ).…”

Section: Resultsmentioning

confidence: 56%

Ddx42p--a human DEAD box protein with RNA chaperone activities

Uhlmann‐Schiffler

Jalal

Stahl

2006

Nucleic Acids Research

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The human gene ddx42 encodes a human DEAD box protein highly homologous to the p68 subfamily of RNA helicases. In HeLa cells, two ddx42 poly(A)+ RNA species were detected both encoding the nuclear localized 938 amino acid Ddx42p polypeptide. Ddx42p has been heterologously expressed and its biochemical properties characterized. It is an RNA binding protein, and ATP and ADP modulate its RNA binding affinity. Ddx42p is an NTPase with a preference for ATP, the hydrolysis of which is enhanced by various RNA substrates. It acts as a non-processive RNA helicase. Interestingly, RNA unwinding by Ddx42p is promoted in the presence of a single-strand (ss) binding protein (T4gp32). Ddx42p, particularly in the ADP-bound form (the state after ATP hydrolysis), also mediates efficient annealing of complementary RNA strands thereby displacing the ss binding protein. Ddx42p therefore represents the first example of a human DEAD box protein possessing RNA helicase, protein displacement and RNA annealing activities. The adenosine nucleotide cofactor bound to Ddx42p apparently acts as a switch that controls the two opposing activities: ATP triggers RNA strand separation, whereas ADP triggers annealing of complementary RNA strands.

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Section: Resultsmentioning

confidence: 56%

Ddx42p--a human DEAD box protein with RNA chaperone activities

Uhlmann‐Schiffler

Jalal

Stahl

2006

Nucleic Acids Research

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“…Our work first identified three MYCT1 interacting proteins. All of them are related to RNA processing [20,24,25]. This might be one of the reasons that MYCT1 is able to recapitulate multiple c-MYC-related phenotypes.…”

Section: Discussionmentioning

confidence: 99%

Transmembrane domain is crucial to the subcellular localization and function of Myc target 1

Gui

Yin

et al. 2015

J Cellular Molecular Medi

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Deregulation of c‐MYC occurs in a variety of human cancers. Overexpression of c‐MYC promotes cell growth, proliferation, apoptosis, transformation and genomic instability. MYC target 1 (MYCT1) is a direct target gene of c‐MYC, and its murine homologue MT‐MC1 recapitulated multiple c‐Myc‐related phenotypes. However, the molecular mechanism of MYCT1 remains unclear. Here, we identified the transmembrane (TM) domain of MYCT1, not the nuclear localization sequence, is indispensable to the vesicle‐associated localization of MYCT1 protein in the cytoplasmic membrane vesicle. Overexpression of MYCT1, not MYCT1 (ΔTM), decreased cell viability under serum deprivation and increased tumour cell migration ability. We further identified CKAP4 interacted with MYCT1 and contributed to the function of MYCT1. In addition, we found that a mutation, A88D, which is observed in patient sample, changed the localization, and abolished the effect on cell viability and cell migration, suggesting that the TM domain is critical to MYCT1.

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“…Consistent with their central roles in nucleic acid metabolic processes, an increasing number of helicases were found to be involved in severe diseases, often associated with significant cancer susceptibility. Autoantibodies to DEAD box protein have been reported in diabetes mellitus, 20 pancreatic cancer, 21 and connective tissue disease. 22 Our study demonstrated that autoantibodies to DEAD box polypeptide 3 were present in sera of patients with HCC.…”

Section: Discussionmentioning

confidence: 99%

Identification of Hepatocellular-Carcinoma-Associated Antigens and Autoantibodies by Serological Proteome Analysis Combined with Protein Microarray

Chen

et al. 2007

J. Proteome Res.

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To comprehensively study autoantibodies in patients with hepatocellular carcinoma (HCC), we used an approach-based serology and proteomics technologies. Total proteins extracted from HepG2 cells and HepG2.2.15 cells were separated by two-dimensional gel electrophoresis (2DE) and then transferred onto polyvinylidene difluoride (PVDF) membranes, which were subsequently incubated with sera from HCC patients or from normal controls. As a result, 13 HCC-associated antigens were identified. Antigenicity of eight proteins was further confirmed using recombinant proteins by Western blotting (WB) and protein microarray. The results of antigen microarray analysis showed strong signals of keratin 8 and lamin A/C in chronic hepatitis controls; therefore, the autoantibodies to keratin 8 and lamin A/C may not be HCC-specific. These two antigens were removed from subsequent analyses. The frequencies of positive reactions to DEAD (Asp-Glu-Ala-Asp) box polypeptide 3, eukaryotic translation elongation factor 2 (eEF2), apoptosis-inducing factor (AIF), heterogeneous nuclear ribonucleoprotein A2 (hnRNP A2), prostatic binding protein, and triosephosphate isomerase (TIM) were significantly higher in HCC than in chronic hepatitis and normal individuals. Positive reactions to DEAD box polypeptide 3, eEF2, AIF, and prostatic binding protein were significantly more frequent in HCC than in any other cancer. The sensitivity of any individual antigen in HCC at stage I ranged from 50 to 85%. When the combinations of six antigens were analyzed, the sensitivity increased to 90%. We conclude that the detection of autoantibodies against the six antigens may have value on early diagnosis of HCC.

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Identification of a novel human member of the DEAD box protein family

Cited by 6 publications

References 21 publications

Ddx42p--a human DEAD box protein with RNA chaperone activities

Ddx42p--a human DEAD box protein with RNA chaperone activities

Transmembrane domain is crucial to the subcellular localization and function of Myc target 1

Identification of Hepatocellular-Carcinoma-Associated Antigens and Autoantibodies by Serological Proteome Analysis Combined with Protein Microarray

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