Characterisation of a novel cysteine/histidine‐rich metal binding domain from <i>Xenopus</i> nuclear factor XNF7

Borden, Katherine L. B.; Martin, Stephen R.; O’Reilly, Nicola; Lally, John M.; Reddy, Bramham A.; Etkin, Laurence D.; Freemont, Paul S.

doi:10.1016/0014-5793(93)80741-c

Cited by 38 publications

(28 citation statements)

References 39 publications

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“…Our previous work has shown that, although there are seven potential metal ligands, the XNF7 B-box peptide binds only one Zn2+ per molecule and the Zn2+ is bound tetrahedrally (24). Therefore, of the seven potential ligands conserved in XNF7 B-box (see Fig.…”

mentioning

confidence: 99%

In vivo and in vitro characterization of the B1 and B2 zinc-binding domains from the acute promyelocytic leukemia protooncoprotein PML.

Borden¹,

Lally²,

Martin³

et al. 1996

Proc. Natl. Acad. Sci. U.S.A.

107

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Acute promyelocytic leukemia (APL) has been ascribed to a chromosomal translocation event which results in a fusion protein comprising the PML protein and retinoic acid receptor a. PML is normally a component of a nuclear multiprotein complex which is disrupted in the APL disease state. Here, two newly defined cysteine/histidine-rich protein motifs called the B-box (Bi and B2) from PML have been characterized in terms of their effect on PML nuclear body formation, their dimerization, and their biophysical properties. We have shown that both peptides bind Zn2+, which induces changes in the peptides' structures. We demonstrate that mutants in both Bi and B2 do not form PML nuclear bodies in vivo and have a phenotype that is different from that observed in the APL disease state. Interestingly, these mutations do not affect the ability of wild-type PML to dimerize with mutant proteins in vitro, suggesting that the Bi and B2 domains are involved in an additional interaction central to PML nuclear body formation. This report in conjunction with our previous work demonstrates that the PML RING-B1/B2 motif plays a fundamental role in formation of a large multiprotein complex, a function that may be common to those unrelated proteins which contain the motif.The human PML gene is associated with APL (acute promyelocytic leukemia), which arises due to a block in normal differentiation of promyelocytes (for review, see ref. 1). In APL cells, PML is fused with the retinoic acid receptor a (RARa) following a reciprocal chromosomal translocation t(15;17)(q22q21) (2-5). The PML protein has been shown to be part of a nuclear multiprotein complex distinct from small nuclear ribonucleoproteins and nucleoli (6-10). These PML nuclear bodies become disrupted in leukemic cells; however, treatment with retinoic acid reverses these changes (8-10). It has been shown that the PML-RARa fusion product can bind to both normal PML (8, 10) as well as RXR, another retinoic acid receptor family member (retinoid X receptor), forming heterodimers (11). This leads to speculation that there is a dominant-negative effect of PML-RARa over both the PML protein and the RXR pathways. PML, but not PML-RARa, has been shown to be a growth suppressor both in vitro and in vivo (12), suggesting that sequestration of normal PML by PML-RARa would affect the growth suppressor activity of PML and sequestration of RXR, the induction of differentiation (12). It is suggested that both events may be necessary for leukemogenesis (12,13).The PML coding sequence contains three novel cysteinerich metal binding regions and a predicted a-helical coiled-coilThe publication costs of this article were defrayed in part by page charge payment. This article must therefore be hereby marked "advertisement" in accordance with 18 U.S.C. §1734 solely to indicate this fact. 1601(see refs. 2 and 14). The first region, the RING motif, defines a family of proteins expressed in organisms ranging from plants to viruses, several of which have been implicated in oncogenesis (for revie...

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mentioning

confidence: 99%

In vivo and in vitro characterization of the B1 and B2 zinc-binding domains from the acute promyelocytic leukemia protooncoprotein PML.

Borden¹,

Lally²,

Martin³

et al. 1996

Proc. Natl. Acad. Sci. U.S.A.

107

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“…Production of soluble B-box proteins is challenging from heterologous expression systems, such as in E. coli (12). We observed that soluble full-length AtBBX32 protein can be expressed by coupled transcription/translation in a wheat germ cell-free system.…”

Section: Resultsmentioning

confidence: 96%

“…The propensity for aggregation and precipitation makes B-box domains poor candidates for crystal structure studies (12). Although there is no plant B-box structure reported, several B-box structures from other species have been determined (34).…”

Section: N-terminal B-box Domain Of Atbbx32 Is Essential For the Bindmentioning

confidence: 99%

“…The consensus sequence of this conserved B-box is CX 2 CX 7-9 CX 2 DX 4 CX 2 CX 3-4 HX 8 H (2). Involvement of conserved Cys and His residues in zinc ligation was illustrated in one-dimensional 1 H NMR studies of the B-box domain from Xenopus nuclear factor-7 (XNF-7) (12,13). However, there has been little biochemical and biophysical characterization of B-box domains from plant B-box proteins.…”

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confidence: 99%

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Involvement of the N-terminal B-box Domain of Arabidopsis BBX32 Protein in Interaction with Soybean BBX62 Protein

Gibson

et al. 2012

Journal of Biological Chemistry

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Background: AtBBX32 is a member of the B-box protein family from A. thaliana. Its molecular mechanism is poorly understood. Results: We demonstrate functional interactions of AtBBX32 with soybean BBX62 (GmBBX62). Conclusion:The N-terminal B-box domain plays a key role in mediating the interaction between AtBBX32 and GmBBX62. Significance: Our data offer novel insight into the role of B-box domains in mediating protein-protein interactions between different plant B-box proteins.

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“…The presence of this domain may provide further insight into the potential mechanism of action of HERF1. In addition to AFP and RFP, whose functions remain unknown, several other RBCC proteins contain an rfp domain: MID1, which is mutated in Opitz syndrome, an inherited human multiorgan disorder primarily affecting midline structures (31); three Xenopus nuclear proteins (xnf7, XL43, and XL75), which are involved in early development (3,30); and the amphibian PwA33 protein, which binds to nascent transcripts on lampbrush chromosome loops in oocytes (1). The rfp domain is also found associated with an immunoglobulin domain in butyrophilin, a secreted protein found in milk (13).…”

Section: Discussionmentioning

confidence: 99%

HERF1, a Novel Hematopoiesis-Specific RING Finger Protein, Is Required for Terminal Differentiation of Erythroid Cells

Harada¹,

Harada²,

O'Brien³

et al. 1999

Molecular and Cellular Biology

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The AML1/core binding factor ␤ (CBF␤) transcription factor is essential for definitive hematopoiesis; however, the downstream pathways through which it functions remain incompletely defined. Using a differential cloning approach to define components of this pathway, we have identified a novel gene designated HERF1 (for hematopoietic RING finger 1), whose expression during development is dependent on the presence of functional AML1/CBF␤. HERF1 contains a tripartite RING finger-B box-␣-helical coiled-coil domain and a C-terminal region homologous to the ret proto-oncogene-encoded finger protein. Expression of HERF1 during embryogenesis coincides with the appearance of definitive erythropoiesis and in adult mice is restricted to erythroid cells, increasing 30-fold during terminal differentiation. Importantly, inhibition of HERF1 expression blocked terminal erythroid differentiation of the murine erythroleukemia cell line MEL, whereas its overexpression induced erythroid maturation. These results suggest an important role for this protein in erythropoiesis.

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Characterisation of a novel cysteine/histidine‐rich metal binding domain from Xenopus nuclear factor XNF7

Cited by 38 publications

References 39 publications

In vivo and in vitro characterization of the B1 and B2 zinc-binding domains from the acute promyelocytic leukemia protooncoprotein PML.

In vivo and in vitro characterization of the B1 and B2 zinc-binding domains from the acute promyelocytic leukemia protooncoprotein PML.

Involvement of the N-terminal B-box Domain of Arabidopsis BBX32 Protein in Interaction with Soybean BBX62 Protein

HERF1, a Novel Hematopoiesis-Specific RING Finger Protein, Is Required for Terminal Differentiation of Erythroid Cells

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