Isolation of human and mouse HMG2a cDNAs: evidence for an HMG2a-specific 3′ untranslated region

Wilke, Klaus; Wiemann, Stefan; Gaul, Renate; Gǒng, Wànkuí; Poustka, Annemarie

doi:10.1016/s0378-1119(97)00324-7

Cited by 15 publications

(8 citation statements)

References 27 publications

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“…at the binding site for H1 in of tandem HMG boxes, not yet tested, is the length of the linker between the boxes : we note that the linker in HMG2a is two bulk nucleosomes. This may be the structural basis for the observations that HMG-D and H1, which are present in abundance at residues shorter [68], and that in human mtTF1 [34] several residues longer, than the linker in HMG1. different developmental stages in Drosophila embryos, appear to be alternative chromosomal components [75], and that HMG1 and H1 may occupy the same binding site on mononucleosomes Insights from competition experiments.…”

Section: Discussionmentioning

confidence: 91%

DNA‐binding properties of the tandem HMG boxes of high‐mobility‐group protein 1 (HMG1)

Grasser¹,

Teo²,

Lee³

et al. 1998

European Journal of Biochemistry

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High-mobility-group protein 1 (HMG1) is a conserved chromosomal protein with two homologous DNA-binding HMG-box domains, A and B, linked by a short basic region to an acidic carboxy-terminal tail. NMR spectroscopy on the free didomain (AB) shows that the two HMG boxes do not interact. The didomain has a higher affinity for all DNA substrates tested than single HMG-box domains and has a significantly higher ability to distort DNA by bending and supercoiling. The interaction of the didomain with DNA is stabilized by the presence of the basic region (Ϸ20 residues, 9 of which are Lys) that links the second HMG box to the acidic tail in intact HMG1; this may be, at least in part, why this region also enhances supercoiling of relaxed circular DNA by the didomain and circularization of short DNA fragments (in the presence of ligase). Competition assays suggest significantly different structure-specific preferences of single and tandem HMG boxes for four-way junction and supercoiled plasmid DNA. Binding to supercoiled DNA appears to be promoted by protein oligomerization, which is pronounced for the didomains. Electron microscopy suggests that the oligomers are globular aggregates, associated with DNA looping. One box versus two (or several) is likely to be an important determinant of the properties of (non-sequence specific) HMG-box proteins.Keywords : high-mobility-group protein 1 (HMG1) ; four-way junction ; DNA bending; supercoiling ; NMR.High-mobility-group proteins 1 and 2 (HMG1 and 2) are cave face of the protein domain [18, 22]

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Section: Discussionmentioning

confidence: 91%

DNA‐binding properties of the tandem HMG boxes of high‐mobility‐group protein 1 (HMG1)

Grasser¹,

Teo²,

Lee³

et al. 1998

European Journal of Biochemistry

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“…015347; Wilke et al, 1997), a member of the High Mobility Group of chromatin-associated proteins. These proteins can act as modulators of transcription through their ability to influence chromatin architecture (reviewed in Wolffe, 1999).…”

Section: E11 (Enhanced Posterior)mentioning

confidence: 99%

Pilot morpholino screen in Xenopus tropicalis identifies a novel gene involved in head development

Kenwrick¹,

Amaya

Papalopulu

2003

Developmental Dynamics

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The diploid frog X. tropicalis has recently been adopted as a model genetic system, but loss-of-function screens in Xenopus have not yet been performed. We have undertaken a pilot functional knockdown screen in X. tropicalis for genes involved in nervous system development by injecting antisense morpholino (MO) oligos directed against X. tropicalis mRNAs. Twenty-six genes with primary expression in the nervous system were selected as targets based on an expression screen previously conducted in X. laevis. Reproducible phenotypes were observed for six and for four of these, a second MO gave a similar result. One of these genes encodes a novel protein with previously unknown function. Knocking down this gene, designated pinhead, results in severe microcephaly, whereas, overexpression results in macrocephaly. Together with the early embryonic expression in the anterior neural plate, these data indicate that pinhead is a novel gene involved in controlling head development. Developmental Dynamics 229:289 -299, 2004.

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“…High-mobility group box 3 (HMGB3), also known as HMG2A, belongs to the HMGB family, which binds to nucleosomes in a sequence-independent manner and participates in DNA repair, replication, transcription, and recombination [ 7 , 8 ]. HMGB3 is highly expressed in stem cells and cancer cells and is rarely transactivated in normal adult tissues, making it a promising therapeutic target [ 9 , 10 ]. HMGB3 is reported to regulate the proper balance between hematopoietic stem cell (HSC) self-renewal and differentiation, and HMGB3 deficiency results in enhanced self-renewal capabilities in HSCs, which can induce the occurrence of leukemia [ 11 ].…”

Section: Introductionmentioning

confidence: 99%

HMGB3 promotes PARP inhibitor resistance through interacting with PARP1 in ovarian cancer

Han

et al. 2022

Cell Death Dis

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Poly (ADP-ribose) polymerase (PARP) inhibitor (PARPi) resistance remains a therapeutic challenge in ovarian cancer. High-mobility group box 3 (HMGB3) plays significant roles in the development of drug resistance of many cancers. However, the function of HMGB3 in PARPi resistance is poorly understood. In the current study, we clarified that HMGB3 was aberrantly overexpressed in high-grade serous ovarian carcinoma (HGSOC) tissues, and high HMGB3 levels indicated shorter overall survival and drug resistance in HGSOC. The overexpression of HMGB3 increased the insensitivity of ovarian cancer to PARPi, whereas HMGB3 knockdown reduced PARPi resistance. Mechanistically, PARP1 was identified as a novel interaction partner of HMGB3, which could be blocked using olaparib and was enhanced upon DNA damage conditions. We further showed that loss of HMGB3 induced PARP1 trapping at DNA lesions and inhibited the PARylation activity of PARP1, resulting in an increased DNA damage response and cell apoptosis. The PARPi-resistant role of HMGB3 was also verified in a xenograft mouse model. In conclusion, HMGB3 promoted PARPi resistance via interacting with PARP1, and the targeted inhibition of HMGB3 might overcome PARPi resistance in ovarian cancer therapy.

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Isolation of human and mouse HMG2a cDNAs: evidence for an HMG2a-specific 3′ untranslated region

Cited by 15 publications

References 27 publications

DNA‐binding properties of the tandem HMG boxes of high‐mobility‐group protein 1 (HMG1)

DNA‐binding properties of the tandem HMG boxes of high‐mobility‐group protein 1 (HMG1)

Pilot morpholino screen in Xenopus tropicalis identifies a novel gene involved in head development

HMGB3 promotes PARP inhibitor resistance through interacting with PARP1 in ovarian cancer

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