A unique bipartite cysteine-histidine motif defines a subfamily of potential zinc-finger proteins

Reddy, Bramham A.; Etkin, Laurence D.

doi:10.1093/nar/19.22.6330

Cited by 82 publications

(46 citation statements)

References 8 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…The 64-kDa ARD1 protein is a member of the tripartite motif (TRIM) family (10), also termed RBCC (11), for RING (12), B-Box zinc finger (13), coiled-coil (14) (Fig. 1 Upper).…”

Section: Rbcc ͉ Trim Protein ͉ Arf ͉ Arf-gapmentioning

confidence: 99%

E3 ubiquitin ligase activity of the trifunctional ARD1 (ADP-ribosylation factor domain protein 1)

Vichi

Payne

Pacheco–Rodriguez

et al. 2005

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

View full text Add to dashboard Cite

Protein ubiquitinylation plays a key role in many important cellular processes. Ubiquitinylation requires the E1 ubiquitin-activating enzyme, an E2 ubiquitin-conjugating enzyme, and, frequently, a substrate-specific E3 ubiquitin-protein ligase. In one class of E3 ubiquitin ligases, the catalytic domain contains a zinc-binding RING finger motif. ARD1 (ADP-ribosylation factor domain protein 1), with a RING finger domain in the N-terminal region, two predicted B-Boxes, and a coiled-coil protein interaction motif immediately preceding an ADP-ribosylation factor domain at the C terminus, belongs to the TRIM (Tripartite motif) or RBCC (RING, B-Box, coiled-coil) family. The region containing the B-Boxes and the coiled-coil motif acts as a GTPase-activating protein for the ADPribosylation factor domain of ARD1. We report here that fulllength ARD1 or the RING finger domain (residues 1-110) produced polyubiquitinylated proteins in vitro in the presence of mammalian E1, an E2 enzyme (UbcH6 or UbcH5a, -5b, or -5c), ATP, and ubiquitin. Deletion of the RING region or point mutations within the RING sequence abolished ARD1 E3 ligase activity. All data are consistent with a potential function for ARD1 as an E3 ubiquitin ligase in cells.RBCC ͉ TRIM protein ͉ ARF ͉ ARF-GAP

show abstract

“…The 64-kDa ARD1 protein is a member of the tripartite motif (TRIM) family (10), also termed RBCC (11), for RING (12), B-Box zinc finger (13), coiled-coil (14) (Fig. 1 Upper).…”

Section: Rbcc ͉ Trim Protein ͉ Arf ͉ Arf-gapmentioning

confidence: 99%

E3 ubiquitin ligase activity of the trifunctional ARD1 (ADP-ribosylation factor domain protein 1)

Vichi

Payne

Pacheco–Rodriguez

et al. 2005

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

View full text Add to dashboard Cite

show abstract

“…We have shown that a peptide corresponding to the RING1 finger domain binds zinc with high affinity and DNA non-s~fic~y in a z~c-de~ndent manner [ 131. Amongst the RING finger family, there are a number of proteins which possess a second cysteine/histidine rich motif C-terminal to the RING finger, termed the B-box domain [15]. The motif is defined as Cys-X(2)-H&X(7)-cys-X(7) -cys-X(2)-Qs " X(5) -His -X(2) -His where X can be any amino acid and the bracketed numbers refer to the number of residues in the intervening sequences, although there are clear preferences for particular amino acids at certain positions between different family members [16].…”

Section: Introductionmentioning

confidence: 99%

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

Borden¹,

Martin²,

O’Reilly

et al. 1993

FEBS Letters

Self Cite

View full text Add to dashboard Cite

A 42 amino acid synthetic peptide corresponding to a newly defined cysteitmkistidine-rich protein motif called B-box, from the Xenopur protein XNF7 has been character&d. The metal-binding stokhiometry and dissociation constant for zinc were determined by competition with the chromopho~c chelator Br,BAPTA, demons~ating that one zinc atom binds per molecule of peptide despite the presence of seven putative metal ligands, and represents the t&t application of this method to measuring zinc stoichiometry of proteins and/or peptides. Cobalt binding studies indicate that the motif binds zinc more tightly than cobalt, that cysteines are used as ligands and that the cation is co-ordinated tetrahedrally. Circular dichroism and NMR studies both indicate that the B-box peptide is structured only in the presence of zinc, copper and to a lesser extent cobalt.

show abstract

“…36 -39). The second signature motif of the RBCC domain is the B-box (40). Two B-box motifs are often found immediately COOH-terminal to the RING finger in the RBCC domain.…”

mentioning

confidence: 99%

Biochemical Analysis of the Kruppel-associated Box (KRAB) Transcriptional Repression Domain

Peng¹,

Begg²,

Harper

et al. 2000

Journal of Biological Chemistry

100

View full text Add to dashboard Cite

The Kruppel-associated box (KRAB) domain is a 75-amino acid transcriptional repressor module commonly found in eukaryotic zinc finger proteins. KRAB-mediated gene silencing requires binding to the RING-B boxcoiled-coil domain of the corepressor KAP-1. Little is known about the biochemical properties of the KRAB domain or the KRAB⅐KAP-1 complex. Using purified components, a combination of biochemical and biophysical analyses has revealed that the KRAB domain from the KOX1 protein is predominantly a monomer and that the KAP-1 protein is predominantly a trimer in solution. The analyses of electrophoretic mobility shift assays, GST association assays, and plasmon resonance interaction data have indicated that the KRAB binding to KAP-1 is direct, highly specific, and high affinity. The optical biosensor data for the complex was fitted to a model of a one-binding step interaction with fast association and slow dissociation rates, with a calculated K d of 142 nM. The fitted R max indicated three molecules of KAP-1 binding to one molecule of the KRAB domain, a stoichiometry that is consistent with quantitative SDSpolyacrylamide gel electrophoresis analysis of the complex. These structural and dynamic parameters of the KRAB/KAP-1 interaction have implications for identifying downstream effectors of KAP-1 silencing and the de novo design of new repression domains.

show abstract

A unique bipartite cysteine-histidine motif defines a subfamily of potential zinc-finger proteins

Cited by 82 publications

References 8 publications

E3 ubiquitin ligase activity of the trifunctional ARD1 (ADP-ribosylation factor domain protein 1)

E3 ubiquitin ligase activity of the trifunctional ARD1 (ADP-ribosylation factor domain protein 1)

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

Biochemical Analysis of the Kruppel-associated Box (KRAB) Transcriptional Repression Domain

Contact Info

Product

Resources

About