Molecular structure of the DNA cross-link repair gene SNM1(PSO2) of the yeast Saccharomyces cerevisiae

Richter, Dorothea; Niegemann, Eckhard; Brendel, Martin

doi:10.1007/bf00279791

Cited by 22 publications

(4 citation statements)

References 34 publications

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“…DNA interstrand cross‐links induce lethal DNA damage, because they block replication, transcription, and segregation of the DNA. SNM1 has been identified in yeast [25] and mammals [26]. However, its relatives have been found from other species within Eukarya and Archaea.…”

Section: Classification Of the Familymentioning

confidence: 99%

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Expansion of the zinc metallo‐hydrolase family of the β‐lactamase fold

Daiyasu¹,

Osaka²,

Ishino³

et al. 2001

FEBS Letters

297

306

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Recently, the zinc metallo-hydrolase family of the L L-lactamase fold has grown quite rapidly, accompanied by the accumulation of sequence and structure data. The variety of the biological functions of the family is higher than expected. In addition, the members often have mosaic structures with additional domains. The family includes class B L L-lactamase, glyoxalase II, arylsulfatase, flavoprotein, cyclase/dehydrase, an mRNA 3P P-processing protein, a DNA cross-link repair enzyme, a DNA uptake-related protein, an alkylphosphonate uptakerelated protein, CMP-N-acetylneuraminate hydroxylase, the romA gene product, alkylsulfatase, and insecticide hydrolases. In this minireview, the functional and structural varieties of the growing protein family are described. ß

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Section: Classification Of the Familymentioning

confidence: 99%

“…However, its relatives have been found from other species within Eukarya and Archaea. It is known that both the fungal and mammalian SNM1s have a zinc finger domain upstream of the β‐lactamase‐like domain [25,26] (see Fig. 3).…”

Section: Classification Of the Familymentioning

confidence: 99%

Expansion of the zinc metallo‐hydrolase family of the β‐lactamase fold

Daiyasu¹,

Osaka²,

Ishino³

et al. 2001

FEBS Letters

297

306

View full text Add to dashboard Cite

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“…For expression and purification of Pso2 protein, a 2734 bp SnaBI-SacI-fragment from pDR3141 [18] was firstly sub-cloned into the SmaI and BamHI sites of pUC18. From the resulting plasmid an internal 2014 bp BglII-BamHI PSO2 ORF containing fragment was cloned into the BamHI site of the vector pGEX-KG (Amersham Biosciences).…”

Section: Over-expression and Purification Of Recombinant Gst-pso2p Anmentioning

confidence: 99%

“…The b-CASP domain consists of a conserved region in the C-terminal moiety that is unique to the PSO2 gene family and is predicted to be a nucleic acid binding domain [11,13,[15][16][17]. The expression of yeast PSO2 mRNA is constitutively low, with approximately 0.3 transcripts/cell [18], but is induced about four times by ICL-inducing agents in exponentially growing cells [19]. Over-expression of PSO2 does not lead to an increased resistance to nitrogen mustard and cisplatin [20].…”

Section: Introductionmentioning

confidence: 99%

Sak1 kinase interacts with Pso2 nuclease in response to DNA damage induced by interstrand crosslink-inducing agents in Saccharomyces cerevisiae

Munari

Revers

Cardone

et al. 2014

Journal of Photochemistry and Photobiology B: Biology

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By isolating putative binding partners through the two-hybrid system (THS) we further extended the characterization of the specific interstrand cross-link (ICL) repair gene PSO2 of Saccharomyces cerevisiae. Nine fusion protein products were isolated for Pso2p using THS, among them the Sak1 kinase, which interacted with the C-terminal β-CASP domain of Pso2p. Comparison of mutagen-sensitivity phenotypes of pso2Δ, sak1Δ and pso2Δsak1Δ disruptants revealed that SAK1 is necessary for complete WT-like repair. The epistatic interaction of both mutant alleles suggests that Sak1p and Pso2p act in the same pathway of controlling sensitivity to DNA-damaging agents. We also observed that Pso2p is phosphorylated by Sak1 kinase in vitro and co-immunoprecipitates with Sak1p after 8-MOP+UVA treatment. Survival data after treatment of pso2Δ, yku70Δ and yku70Δpso2Δ with nitrogen mustard, PSO2 and SAK1 with YKU70 or DNL4 single-, double- and triple mutants with 8-MOP+UVA indicated that ICL repair is independent of YKu70p and DNL4p in S. cerevisiae. Furthermore, a non-epistatic interaction was observed between MRE11, PSO2 and SAK1 genes after ICL induction, indicating that their encoded proteins act on the same substrate, but in distinct repair pathways. In contrast, an epistatic interaction was observed for PSO2 and RAD52, PSO2 and RAD50, PSO2 and XRS2 genes in 8-MOP+UVA treated exponentially growing cells.

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