The COP9 signalosome is an essential regulator of development in the filamentous fungus <i>Aspergillus nidulans</i>

Busch, Silke; Eckert, Sabine; Krappmann, Sven; Braus, Gerhard H.

doi:10.1046/j.1365-2958.2003.03612.x

Cited by 145 publications

(193 citation statements)

References 60 publications

Supporting

Mentioning

179

Contrasting

Unclassified

Order By: Relevance

“…Southern hybridization was performed according to standard protocols (Busch et al, 2003) with nonradioactively labeled probes (Amersham Bioscience, Buckinghamshire, UK). For probe preparations, DNAs were amplified from genomic DNA by PCR using primers listed in Tables S5 and S6. 2.7.…”

Section: Southern Hybridizationmentioning

confidence: 99%

Fungal S-adenosylmethionine synthetase and the control of development and secondary metabolism in Aspergillus nidulans

Gerke

Bayram

Braus

2012

Fungal Genetics and Biology

Self Cite

View full text Add to dashboard Cite

a b s t r a c tThe filamentous fungus Aspergillus nidulans carries a single gene for the S-adenosylmethionine (SAM) synthetase SasA, whereas many other organisms possess multiple SAM synthetases. The conserved enzyme catalyzes the reaction of methionine and ATP to the ubiquitous methyl group donor SAM. SAM is the main methyl group donor for methyltransferases to modify DNA, RNA, protein, metabolites, or phospholipid target substrates. We show here that the single A. nidulans SAM synthetase encoding gene sasA is essential. Overexpression of sasA, encoding a predominantly cytoplasmic protein, led to impaired development including only small sterile fruiting bodies which are surrounded by unusually pigmented auxiliary Hülle cells. Hülle cells are the only fungal cell type which does not contain significant amounts of SasA. Sterigmatocystin production is altered when sasA is overexpressed, suggesting defects in coordination of development and secondary metabolism. SasA interacts with various metabolic proteins including methionine or mitochondrial metabolic enzymes as well as proteins involved in fungal morphogenesis. SasA interaction to histone-2B might reflect a putative epigenetic link to gene expression. Our data suggest a distinct role of SasA in coordinating fungal secondary metabolism and development.

show abstract

Section: Southern Hybridizationmentioning

confidence: 99%

Fungal S-adenosylmethionine synthetase and the control of development and secondary metabolism in Aspergillus nidulans

Gerke

Bayram

Braus

2012

Fungal Genetics and Biology

Self Cite

View full text Add to dashboard Cite

show abstract

“…The FGSC A4 strain served as the wild-type recipient for deletion of cryA, and strains AGB152 and AAH14 (uvsB⌬) were used for overexpression and subcellular localization experiments (Hofmann and Harris, 2000;Busch et al, 2003). Standard laboratory Escherichia coli strains DH5␣ and MACH-1 (Invitrogen) were used for preparation of plasmid DNA.…”

Section: Strains Media and Growth Conditionsmentioning

confidence: 99%

More Than a Repair Enzyme:Aspergillus nidulansPhotolyase-like CryA Is a Regulator of Sexual Development

Bayram

Biesemann

Krappmann

et al. 2008

MBoC

Self Cite

126

115

View full text Add to dashboard Cite

Cryptochromes are blue-light receptors that have presumably evolved from the DNA photolyase protein family, and the genomes of many organisms contain genes for both types of molecules. Both protein structures resemble each other, which suggests that light control and light protection share a common ancient origin. In the genome of the filamentous fungus Aspergillus nidulans, however, only one cryptochrome/photolyase-encoding gene, termed cryA, was identified. Deletion of the cryA gene triggers sexual differentiation under inappropriate culture conditions and results in upregulation of transcripts encoding regulators of fruiting body formation. CryA is a protein whose N-and C-terminal synthetic green fluorescent protein fusions localize to the nucleus. CryA represses sexual development under UVA 350-370 nm light both on plates and in submerged culture. Strikingly, CryA exhibits photorepair activity as demonstrated by heterologous complementation of a DNA repair-deficient Escherichia coli strain as well as overexpression in an A. nidulans uvsB⌬ genetic background. This is in contrast to the single deletion cryA⌬ strain, which does not show increased sensitivity toward UV-induced damage. In A. nidulans, cryA encodes a novel type of cryptochrome/photolyase that exhibits a regulatory function during light-dependent development and DNA repair activity. This represents a paradigm for the evolutionary transition between photolyases and cryptochromes. INTRODUCTIONCryptochromes (CRYs) are blue-light receptors that regulate growth, development, and the circadian clock in higher eukaryotes and that are believed to have evolved from the DNA photolyase protein family (Daiyasu et al., 2004;Lin and Todo, 2005). Photolyases, in contrast, repair UV-induced DNA damage by using a mechanism referred to as photorepair. They absorb light in the blue spectrum and transfer an excited electron from the cofactor FAD to an enzyme-bound cyclobutane pyrimidine dimer (CPD), which is thereby cleaved (Sancar, 1990(Sancar, , 1994Sancar, 1994). Cryptochromes are characterized by an N-terminal photolyase-related (PHR) region without significant photorepair activity and by a C-terminal domain of varying length, which is absent in members of the CRY-DASH subfamily (Daiyasu et al., 2004). The exact function of the CRY-DASH proteins was elusive; however, recent data imply that they are actually photolyases that specifically repair CPDs in single-stranded DNA (Selby and Sancar, 2006). The PHR domain is the most conserved region of the CRY proteins and contains the cofactor FAD required for electron transfer reactions. In Xenopus and Drosophila, the PHR domain is physiologically active even in the absence of the C-terminal domain. The C-terminal domain is important for either localization or protein stability, and its expression in Arabidopsis results in constitutive growth (Lin and Todo, 2005). Plant CRYs are phosphorylated under illumination, and gene expression control ranges from protein interactions to direct chromatin interactions (Shalitin et al....

show abstract

“…The remaining two CSN subunits, CSN5 and CSN6, are not represented by any of the COP/DET/FUS loci because they are encoded by two small gene families, each composed of two genes (Kwok et al, 1998;Peng et al, 2001b). The subsequent identification of the CSN in many other eukaryotic organisms revealed the conservation of this complex throughout evolution (Chamovitz et al, 1996;Seeger et al, 1998;Freilich et al, 1999;Karniol et al, 1999;Mundt et al, 1999;Busch et al, 2003). Interestingly, six of the eight subunits of the CSN contain a PCI (for Proteasome, COP9, Initiation factor 3) domain, whereas the other two (CSN5 and CSN6) contain a MPN/MOV34 (for Mpr1p and Pad1p N-terminal) domain (Aravind and Ponting, 1998;Hofmann and Bucher, 1998;Ponting et al, 1999).…”

Section: Introductionmentioning

confidence: 99%

The Arabidopsis CSN5A and CSN5B Subunits Are Present in Distinct COP9 Signalosome Complexes, and Mutations in Their JAMM Domains Exhibit Differential Dominant Negative Effects on Development

2004

View full text Add to dashboard Cite

The COP9 signalosome (CSN) is an evolutionarily conserved multisubunit protein complex involved in a variety of signaling and developmental processes through the regulation of protein ubiquitination and degradation. A known biochemical role attributed to CSN is a metalloprotease activity responsible for the derubylation of cullins, core components for several types of ubiquitin E3 ligases. The CSN's derubylation catalytic center resides in its subunit 5, which in Arabidopsis thaliana is encoded by two homologous genes, CSN5A and CSN5B. Here, we show that CSN5A and CSN5B subunits are assembled into distinct CSN complexes in vivo, which are present in drastically different abundances, with CSN CSN5A appearing to be the dominant one. Transgenic CSN5A and CSN5B proteins carrying a collection of single mutations in or surrounding the metalloprotease catalytic center are properly assembled into CSN complexes, but only mutations in CSN5A result in a pleiotropic dominant negative phenotype. The extent of phenotypic effects caused by mutations in CSN5A is reflected at the molecular level by impairment in Cullin1 derubylation. These results reveal that three key metal binding residues as well as two other amino acids outside the catalytic center play important roles in CSN derubylation activity. Taken together, our data provide physiological evidence on a positive role of CSN in the regulation of Arabidopsis SCF (for Skp1-Cullin-F-box) E3 ligases through RUB (for Related to Ubiquitin) deconjugation and highlight the unequal role that CSN CSN5A and CSN CSN5B play in controlling the cellular derubylation of cullins. The initial characterization of CSN5A and CSN5B insertion mutants further supports these findings and provides genetic evidence on their unequal role in plant development.

show abstract

The COP9 signalosome is an essential regulator of development in the filamentous fungus Aspergillus nidulans

Cited by 145 publications

References 60 publications

Fungal S-adenosylmethionine synthetase and the control of development and secondary metabolism in Aspergillus nidulans

Fungal S-adenosylmethionine synthetase and the control of development and secondary metabolism in Aspergillus nidulans

More Than a Repair Enzyme:Aspergillus nidulansPhotolyase-like CryA Is a Regulator of Sexual Development

The Arabidopsis CSN5A and CSN5B Subunits Are Present in Distinct COP9 Signalosome Complexes, and Mutations in Their JAMM Domains Exhibit Differential Dominant Negative Effects on Development

Contact Info

Product

Resources

About