LAMMER kinase contributes to genome stability in Ustilago maydis
Аутори
de Sena-Tomas, CarmenSutherland, Jeanette H.
Milisavljević, Mira
Nikolić, Dragana
Perez-Martin, Jose
Kojić, Milorad
Holloman, William K.
Чланак у часопису (Рецензирана верзија)
Метаподаци
Приказ свих података о документуАпстракт
Here we report identification of the lkh1 gene encoding a LAMMER kinase homolog (Lkh1) from a screen for DNA repair-deficient mutants in Ustilago maydis. The mutant allele isolated results from a mutation at glutamine codon 488 to a stop codon that would be predicted to lead to truncation of the carboxyterminal kinase domain of the protein. This mutant (lkh1(Q488*)) is highly sensitive to ultraviolet light, methyl methanesulfonate, and hydroxyurea. In contrast, a null mutant (lkh1 Delta) deleted of the entire lkh1 gene has a less severe phenotype. No epistasis was observed when an lkh1(Q488*) rad51 Delta double mutant was tested for genotoxin sensitivity. However, overexpressing the gene for Rad51, its regulator Brh2, or the Brh2 regulator Dss1 partially restored genotoxin resistance of the lkh1 Delta and lkh1(Q488*) mutants. Deletion of lkh1 in a chk1 Delta mutant enabled these double mutant cells to continue to cycle when challenged with hydroxyurea. lkh1 Delta and lkh1(Q488*) mutant...s were able to complete the meiotic process but exhibited reduced heteroallelic recombination and aberrant chromosome segregation. The observations suggest that Lkh1 serves in some aspect of cell cycle regulation after DNA damage or replication stress and that it also contributes to proper chromosome segregation in meiosis.
Извор:
DNA Repair, 2015, 33, 70-77Издавач:
- Amsterdam : Elsevier
Финансирање / пројекти:
- National Institutes of Health [GM042482, GM079859]
- Молекуларни механизми одговора биљака на абиотички стрес-улога транскрипционих фактора и малих РНК и анализа генетичког диверзитета биљних култура од интереса за пољопривреду и биотехнологију (RS-MESTD-Basic Research (BR or ON)-173005)
- Spanish government [BIO2014-55398-R]
- NATIONAL INSTITUTE OF GENERAL MEDICAL SCIENCES [R01GM079859, R01GM042482] Funding Source: NIH RePORTER
Напомена:
- This is the peer reviewed version of the paper: de Sena-Tomás, C., Sutherland, J. H., Milisavljevic, M., Nikolic, D. B., Pérez-Martín, J., Kojic, M., & Holloman, W. K. (2015). LAMMER kinase contributes to genome stability in Ustilago maydis. DNA Repair, 33, 70–77. https://doi.org/10.1016/j.dnarep.2015.05.011
- Published version: https://imagine.imgge.bg.ac.rs/handle/123456789/887
Повезане информације:
- Друга верзија
https://imagine.imgge.bg.ac.rs/handle/123456789/887 - Друга верзија
https://doi.org/10.1016/j.dnarep.2015.05.011
DOI: 10.1016/j.dnarep.2015.05.011
ISSN: 1568-7864
PubMed: 26176563
WoS: 000359885100007
Scopus: 2-s2.0-84938632585
Институција/група
Institut za molekularnu genetiku i genetičko inženjerstvoTY - JOUR AU - de Sena-Tomas, Carmen AU - Sutherland, Jeanette H. AU - Milisavljević, Mira AU - Nikolić, Dragana AU - Perez-Martin, Jose AU - Kojić, Milorad AU - Holloman, William K. PY - 2015 UR - https://imagine.imgge.bg.ac.rs/handle/123456789/1624 AB - Here we report identification of the lkh1 gene encoding a LAMMER kinase homolog (Lkh1) from a screen for DNA repair-deficient mutants in Ustilago maydis. The mutant allele isolated results from a mutation at glutamine codon 488 to a stop codon that would be predicted to lead to truncation of the carboxyterminal kinase domain of the protein. This mutant (lkh1(Q488*)) is highly sensitive to ultraviolet light, methyl methanesulfonate, and hydroxyurea. In contrast, a null mutant (lkh1 Delta) deleted of the entire lkh1 gene has a less severe phenotype. No epistasis was observed when an lkh1(Q488*) rad51 Delta double mutant was tested for genotoxin sensitivity. However, overexpressing the gene for Rad51, its regulator Brh2, or the Brh2 regulator Dss1 partially restored genotoxin resistance of the lkh1 Delta and lkh1(Q488*) mutants. Deletion of lkh1 in a chk1 Delta mutant enabled these double mutant cells to continue to cycle when challenged with hydroxyurea. lkh1 Delta and lkh1(Q488*) mutants were able to complete the meiotic process but exhibited reduced heteroallelic recombination and aberrant chromosome segregation. The observations suggest that Lkh1 serves in some aspect of cell cycle regulation after DNA damage or replication stress and that it also contributes to proper chromosome segregation in meiosis. PB - Amsterdam : Elsevier T2 - DNA Repair T1 - LAMMER kinase contributes to genome stability in Ustilago maydis EP - 77 SP - 70 VL - 33 DO - 10.1016/j.dnarep.2015.05.011 ER -
@article{ author = "de Sena-Tomas, Carmen and Sutherland, Jeanette H. and Milisavljević, Mira and Nikolić, Dragana and Perez-Martin, Jose and Kojić, Milorad and Holloman, William K.", year = "2015", abstract = "Here we report identification of the lkh1 gene encoding a LAMMER kinase homolog (Lkh1) from a screen for DNA repair-deficient mutants in Ustilago maydis. The mutant allele isolated results from a mutation at glutamine codon 488 to a stop codon that would be predicted to lead to truncation of the carboxyterminal kinase domain of the protein. This mutant (lkh1(Q488*)) is highly sensitive to ultraviolet light, methyl methanesulfonate, and hydroxyurea. In contrast, a null mutant (lkh1 Delta) deleted of the entire lkh1 gene has a less severe phenotype. No epistasis was observed when an lkh1(Q488*) rad51 Delta double mutant was tested for genotoxin sensitivity. However, overexpressing the gene for Rad51, its regulator Brh2, or the Brh2 regulator Dss1 partially restored genotoxin resistance of the lkh1 Delta and lkh1(Q488*) mutants. Deletion of lkh1 in a chk1 Delta mutant enabled these double mutant cells to continue to cycle when challenged with hydroxyurea. lkh1 Delta and lkh1(Q488*) mutants were able to complete the meiotic process but exhibited reduced heteroallelic recombination and aberrant chromosome segregation. The observations suggest that Lkh1 serves in some aspect of cell cycle regulation after DNA damage or replication stress and that it also contributes to proper chromosome segregation in meiosis.", publisher = "Amsterdam : Elsevier", journal = "DNA Repair", title = "LAMMER kinase contributes to genome stability in Ustilago maydis", pages = "77-70", volume = "33", doi = "10.1016/j.dnarep.2015.05.011" }
de Sena-Tomas, C., Sutherland, J. H., Milisavljević, M., Nikolić, D., Perez-Martin, J., Kojić, M.,& Holloman, W. K.. (2015). LAMMER kinase contributes to genome stability in Ustilago maydis. in DNA Repair Amsterdam : Elsevier., 33, 70-77. https://doi.org/10.1016/j.dnarep.2015.05.011
de Sena-Tomas C, Sutherland JH, Milisavljević M, Nikolić D, Perez-Martin J, Kojić M, Holloman WK. LAMMER kinase contributes to genome stability in Ustilago maydis. in DNA Repair. 2015;33:70-77. doi:10.1016/j.dnarep.2015.05.011 .
de Sena-Tomas, Carmen, Sutherland, Jeanette H., Milisavljević, Mira, Nikolić, Dragana, Perez-Martin, Jose, Kojić, Milorad, Holloman, William K., "LAMMER kinase contributes to genome stability in Ustilago maydis" in DNA Repair, 33 (2015):70-77, https://doi.org/10.1016/j.dnarep.2015.05.011 . .