Relationship between endoplasmic reticulum- and Golgi-associated calcium homeostasis and 4-NQO-induced DNA repair in Saccharomyces cerevisiae

Calcium (Ca²⁺) is an important ion that is necessary for the activation of different DNA repair mechanisms. However, the mechanism by which DNA repair and Ca²⁺ homeostasis cooperate remains unclear. We undertook a systems biology approach to verify the relationship between proteins associated with C...

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Bibliographic Details
Published in:Archives of microbiology 2010-04, Vol.192 (4), p.247-257
Main Authors: Poletto, Nadine Paese, Henriques, João Antonio Pêgas, Bonatto, Diego
Format: Article
Language:English
Subjects:
4-Nitroquinoline-1-oxide - pharmacology
Biochemistry
Biological and medical sciences
Biology
Biomedical and Life Sciences
Biotechnology
Calcium - metabolism
Calcium-Transporting ATPases - metabolism
Cell Biology
Cell Cycle
Cell death
DNA repair
DNA Repair - drug effects
DNA-Binding Proteins - metabolism
Ecology
Endoplasmic reticulum
Endoplasmic Reticulum - metabolism
Fundamental and applied biological sciences. Psychology
Gene Deletion
Golgi Apparatus - metabolism
Homeostasis
Life Sciences
Membrane Transport Proteins - metabolism
Microbial Ecology
Microbiology
Miscellaneous
Molecular Chaperones
Mutagenesis
Mycology
Ontology
Original Paper
Protein Interaction Mapping
Proteins
Saccharomyces cerevisiae - genetics
Saccharomyces cerevisiae - metabolism
Saccharomyces cerevisiae Proteins - metabolism
Software
Systems Biology
Yeast
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Summary:Calcium (Ca²⁺) is an important ion that is necessary for the activation of different DNA repair mechanisms. However, the mechanism by which DNA repair and Ca²⁺ homeostasis cooperate remains unclear. We undertook a systems biology approach to verify the relationship between proteins associated with Ca²⁺ homeostasis and DNA repair for Saccharomyces cerevisiae. Our data indicate that Pmr1p, a Ca²⁺ transporter of Golgi complex, interacts with Cod1p, which regulates Ca²⁺ levels in the endoplasmic reticulum (ER), and with Rad4p, which is a nucleotide excision repair (NER) protein. This information was used to construct single and double mutants defective for Pmr1p, Cod1p, and Rad4p followed by cytotoxic, cytostatic, and cell cycle arrest analyses after cell exposure to different concentrations of 4-nitroquinoline 1-oxide (4-NQO). The results indicated that cod1Δ, cod1Δrad4Δ, and cod1Δpmr1Δ strains have an elevated sensitivity to 4-NQO when compared to its wild-type (WT) strain. Moreover, both cod1Δpmr1Δ and cod1Δrad4Δ strains have a strong arrest at G₂/M phases of cell cycle after 4-NQO treatment, while pmr1Δrad4Δ have a similar sensitivity and cell cycle arrest profile when compared to rad4Δ after 4-NQO exposure. Taken together, our results indicate that deletion in Golgi- and ER-associated Ca²⁺ transporters affect the repair of 4-NQO-induced DNA damage.
ISSN:0302-8933
1432-072X
DOI:10.1007/s00203-010-0553-0