Structure and function of PCD/DCoH, an enzyme with regulatory properties

Suck, Dietrich; Ficner, Ralf

doi:10.1016/0014-5793(96)00573-x

Cited by 20 publications

(18 citation statements)

References 32 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…HNF-1␣ is a modular protein containing at least four functional regions: an N-terminal dimerization domain, bipartite DNA-binding domain, and C-terminal transcriptional activation region (16)(17)(18)(19). The N-terminal domain, an autonomous module flexibly linked to the DNAbinding domain (18,19), also functions as a target of transcriptional coactivator dimerization cofactor of homeodomains (DCoH) (20)(21)(22)(23)(24)(25)(26)(27)(28). MODY-associated mutations occur in each domain (4,(8)(9)(10)(11)(12)(13).…”

mentioning

confidence: 99%

Diabetes-associated mutations in a β-cell transcription factor destabilize an antiparallel “mini-zipper” in a dimerization interface

Hua

Zhao

Narayana

et al. 2000

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

View full text Add to dashboard Cite

Maturity-onset diabetes of the young, a monogenic form of Type II diabetes mellitus, is most commonly caused by mutations in hepatic nuclear factor 1α (HNF-1α). Here, the dimerization motif of HNF-1α is shown to form an intermolecular four-helix bundle. One face contains an antiparallel coiled coil whereas the other contains splayed α-helices. The “mini-zipper” is complementary in structure and symmetry to the top surface of a transcriptional coactivator (dimerization cofactor of homeodomains). The bundle is destabilized by a subset of mutations associated with maturity-onset diabetes of the young. Impaired dimerization of a β-cell transcription factor thus provides a molecular mechanism of metabolic deregulation in diabetes mellitus.

show abstract

mentioning

confidence: 99%

Diabetes-associated mutations in a β-cell transcription factor destabilize an antiparallel “mini-zipper” in a dimerization interface

Hua

Zhao

Narayana

et al. 2000

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

View full text Add to dashboard Cite

show abstract

“…The function of SDIRIP1 remained unknown. In mammals, the single copy of PCD functions as a bifunctional protein, as both a metabolic enzyme and a nuclear cofactor in transcriptional regulation (Suck and Ficner, 1996). It has been reported that in Arabidopsis protoplasts, SDIRIP1-GFP was localized exclusively to the chloroplast (Naponelli et al, 2008).…”

Section: Sdirip1 Interacts With Sdir1 In Vivomentioning

confidence: 99%

“…The sole copy of PCD/DCoH has PCD activity in the mitochondria and also acts as DCoH in the nucleus in mammals (Suck and Ficner, 1996). Plants contain two copies of PCD/DCoH homologs (Naponelli et al, 2008).…”

Section: Sdirip1 Is Localized To the Chloroplast Cell Periphery Andmentioning

confidence: 99%

The RING Finger Ubiquitin E3 Ligase SDIR1 Targets SDIR1-INTERACTING PROTEIN1 for Degradation to Modulate the Salt Stress Response and ABA Signaling inArabidopsis

et al. 2015

View full text Add to dashboard Cite

The plant hormone abscisic acid (ABA) regulates many aspects of plant development and the stress response. The intracellular E3 ligase SDIR1 (SALT-AND DROUGHT-INDUCED REALLY INTERESTING NEW GENE FINGER1) plays a key role in ABA signaling, regulating ABA-related seed germination and the stress response. In this study, we found that SDIR1 is localized on the endoplasmic reticulum membrane in Arabidopsis thaliana. Using cell biology, molecular biology, and biochemistry approaches, we demonstrated that SDIR1 interacts with and ubiquitinates its substrate, SDIRIP1 (SDIR1-INTERACTING PROTEIN1), to modulate SDIRIP1 stability through the 26S proteasome pathway. SDIRIP1 acts genetically downstream of SDIR1 in ABA and salt stress signaling. In detail, SDIRIP1 selectively regulates the expression of the downstream basic region/leucine zipper motif transcription factor gene ABA-INSENSITIVE5, rather than ABA-RESPONSIVE ELEMENTS BINDING FACTOR3 (ABF3) or ABF4, to regulate ABA-mediated seed germination and the plant salt response. Overall, the SDIR1/SDIRIP1 complex plays a vital role in ABA signaling through the ubiquitination pathway.

show abstract

“…Crystal structures, sequences, and site-directed mutagenesis of animal and P. aeruginosa PCDs point to a canonical catalytic motif, [DE] Hulo et al, 2006), in which the three His residues are particularly critical (Cronk et al, 1996;Kö ster et al, 1996Kö ster et al, , 1998Suck and Ficner, 1996;Rebrin et al, 1998). Crystal structures also establish that mammalian PCD is a tetramer with a ''dimers of dimers'' configuration, whereas bacterial PCDs are dimers Rose et al, 2004).…”

mentioning

confidence: 99%

“…Crystal structures also establish that mammalian PCD is a tetramer with a ''dimers of dimers'' configuration, whereas bacterial PCDs are dimers Rose et al, 2004). The tetramerization relates to a second function of mammalian PCD as a transcriptional coactivator that binds to, and enhances activity of, HNF1 transcription factors; this nonmetabolic function is termed Dimerization Cofactor of HNF1 (DCoH; Suck and Ficner, 1996). DCoH activity is unrelated to PCD activity; the HNF1 and pterin binding sites are separate, and complex formation with HNF1 does not affect PCD activity (Rhee et al, 1997).…”

mentioning

confidence: 99%

Phylogenomic and Functional Analysis of Pterin-4a-Carbinolamine Dehydratase Family (COG2154) Proteins in Plants and Microorganisms

et al. 2008

View full text Add to dashboard Cite

Pterin-4a-carbinolamine dehydratases (PCDs) recycle oxidized pterin cofactors generated by aromatic amino acid hydroxylases (AAHs). PCDs are known biochemically only from animals and one bacterium, but PCD-like proteins (COG2154 in the Clusters of Orthologous Groups [COGs] database) are encoded by many plant and microbial genomes. Because these genomes often encode no AAH homologs, the annotation of their COG2154 proteins as PCDs is questionable. Moreover, some COG2154 proteins lack canonical residues that are catalytically important in mammalian PCDs. Diverse COG2154 proteins of plant, fungal, protistan, and prokaryotic origin were therefore tested for PCD activity by functional complementation in Escherichia coli, and the plant proteins were localized using green fluorescent protein fusions. Higher and lower plants proved to have two COG2154 proteins, a mitochondrial one with PCD activity and a noncanonical, plastidial one without. Phylogenetic analysis indicated that the latter is unique to plants and arose from the former early in the plant lineage. All 10 microbial COG2154 proteins tested had PCD activity; six of these came from genomes with no AAH, and six were noncanonical. The results suggested the motif [EDKH]-x(3)-H-[HN]-[PCS]-x(5,6)-[YWF]-x(9)-[HW]-x(8,15)-D as a signature for PCD activity. Organisms having a functional PCD but no AAH partner include angiosperms, yeast, and various prokaryotes. In these cases, PCD presumably has another function. An ancillary role in molybdopterin cofactor metabolism, hypothesized from phylogenomic evidence, was supported by demonstrating significantly lowered activities of two molybdoenzymes in Arabidopsis thaliana PCD knockout mutants. Besides this role, we propose that partnerless PCDs support the function of as yet unrecognized pterin-dependent enzymes.

show abstract

Structure and function of PCD/DCoH, an enzyme with regulatory properties

Cited by 20 publications

References 32 publications

Diabetes-associated mutations in a β-cell transcription factor destabilize an antiparallel “mini-zipper” in a dimerization interface

Diabetes-associated mutations in a β-cell transcription factor destabilize an antiparallel “mini-zipper” in a dimerization interface

The RING Finger Ubiquitin E3 Ligase SDIR1 Targets SDIR1-INTERACTING PROTEIN1 for Degradation to Modulate the Salt Stress Response and ABA Signaling inArabidopsis

Phylogenomic and Functional Analysis of Pterin-4a-Carbinolamine Dehydratase Family (COG2154) Proteins in Plants and Microorganisms

Contact Info

Product

Resources

About