A novel C-terminal domain of RecJ is critical for interaction with HerA in Deinococcus radiodurans
Homologous recombination (HR) generates error-free repair products, which plays an important role in double strand break repair and replication fork rescue processes. DNA end resection, the critical step in HR, is usually performed by a series of nuclease/helicase. RecJ was identified as a 5’-3’ exo...
| Main Authors: | , , , , , , , |
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| Format: | Article |
| Language: | English |
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Frontiers Media S.A.
2015-11-01
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| Series: | Frontiers in Microbiology |
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| Online Access: | http://journal.frontiersin.org/Journal/10.3389/fmicb.2015.01302/full |
| _version_ | 1819291865298501632 |
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| author | Kaiying eCheng Ye eZhao Xuanyi eChen Tao eLi Liangyan eWang Hong eXu Bing eTian Yuejin eHua |
| author_facet | Kaiying eCheng Ye eZhao Xuanyi eChen Tao eLi Liangyan eWang Hong eXu Bing eTian Yuejin eHua |
| author_sort | Kaiying eCheng |
| collection | DOAJ |
| description | Homologous recombination (HR) generates error-free repair products, which plays an important role in double strand break repair and replication fork rescue processes. DNA end resection, the critical step in HR, is usually performed by a series of nuclease/helicase. RecJ was identified as a 5’-3’ exonuclease involved in bacterial DNA end resection. Typical RecJ possesses a conserved DHH domain, a DHHA1 domain, and an oligonucleotide/oligosaccharide-binding (OB) fold. However, RecJs from Deinococcus-Thermus phylum, such as Deinococcus radiodurans RecJ (DrRecJ), possess an extra C-terminal domain (CTD), of which the function has not been characterized. Here, we showed that a CTD-deletion of DrRecJ (DrRecJΔC) could not restore drrecJ mutant growth and mitomycin C (MMC)-sensitive phenotypes, indicating that this domain is essential for DrRecJ in vivo. DrRecJΔC displayed reduced DNA nuclease activity and DNA binding ability. Direct interaction was identified between DrRecJ-CTD and DrHerA, which stimulates DrRecJ nuclease activity by enhancing its DNA binding affinity. Moreover, DrNurA nuclease, another partner of DrHerA, inhibited the stimulation of DrHerA on DrRecJ nuclease activity by interaction with DrHerA. Opposing growth and MMC-resistance phenotypes between the recJ and nurA mutants were observed. A novel modulation mechanism among DrRecJ, DrHerA, and DrNurA was also suggested. |
| first_indexed | 2024-12-24T03:45:25Z |
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| id | doaj.art-3c111e7b491c4d4bbcee337543988960 |
| institution | Directory Open Access Journal |
| issn | 1664-302X |
| language | English |
| last_indexed | 2024-12-24T03:45:25Z |
| publishDate | 2015-11-01 |
| publisher | Frontiers Media S.A. |
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| series | Frontiers in Microbiology |
| spelling | doaj.art-3c111e7b491c4d4bbcee3375439889602022-12-21T17:16:44ZengFrontiers Media S.A.Frontiers in Microbiology1664-302X2015-11-01610.3389/fmicb.2015.01302156386A novel C-terminal domain of RecJ is critical for interaction with HerA in Deinococcus radioduransKaiying eCheng0Ye eZhao1Xuanyi eChen2Tao eLi3Liangyan eWang4Hong eXu5Bing eTian6Yuejin eHua7Key Laboratory of Chinese Ministry of Agriculture for Nuclear-Agricultural Sciences, Institute of Nuclear-Agricultural Sciences, Zhejiang UniversityKey Laboratory of Chinese Ministry of Agriculture for Nuclear-Agricultural Sciences, Institute of Nuclear-Agricultural Sciences, Zhejiang UniversityKey Laboratory of Chinese Ministry of Agriculture for Nuclear-Agricultural Sciences, Institute of Nuclear-Agricultural Sciences, Zhejiang UniversityKey Laboratory of Chinese Ministry of Agriculture for Nuclear-Agricultural Sciences, Institute of Nuclear-Agricultural Sciences, Zhejiang UniversityKey Laboratory of Chinese Ministry of Agriculture for Nuclear-Agricultural Sciences, Institute of Nuclear-Agricultural Sciences, Zhejiang UniversityKey Laboratory of Chinese Ministry of Agriculture for Nuclear-Agricultural Sciences, Institute of Nuclear-Agricultural Sciences, Zhejiang UniversityKey Laboratory of Chinese Ministry of Agriculture for Nuclear-Agricultural Sciences, Institute of Nuclear-Agricultural Sciences, Zhejiang UniversityKey Laboratory of Chinese Ministry of Agriculture for Nuclear-Agricultural Sciences, Institute of Nuclear-Agricultural Sciences, Zhejiang UniversityHomologous recombination (HR) generates error-free repair products, which plays an important role in double strand break repair and replication fork rescue processes. DNA end resection, the critical step in HR, is usually performed by a series of nuclease/helicase. RecJ was identified as a 5’-3’ exonuclease involved in bacterial DNA end resection. Typical RecJ possesses a conserved DHH domain, a DHHA1 domain, and an oligonucleotide/oligosaccharide-binding (OB) fold. However, RecJs from Deinococcus-Thermus phylum, such as Deinococcus radiodurans RecJ (DrRecJ), possess an extra C-terminal domain (CTD), of which the function has not been characterized. Here, we showed that a CTD-deletion of DrRecJ (DrRecJΔC) could not restore drrecJ mutant growth and mitomycin C (MMC)-sensitive phenotypes, indicating that this domain is essential for DrRecJ in vivo. DrRecJΔC displayed reduced DNA nuclease activity and DNA binding ability. Direct interaction was identified between DrRecJ-CTD and DrHerA, which stimulates DrRecJ nuclease activity by enhancing its DNA binding affinity. Moreover, DrNurA nuclease, another partner of DrHerA, inhibited the stimulation of DrHerA on DrRecJ nuclease activity by interaction with DrHerA. Opposing growth and MMC-resistance phenotypes between the recJ and nurA mutants were observed. A novel modulation mechanism among DrRecJ, DrHerA, and DrNurA was also suggested.http://journal.frontiersin.org/Journal/10.3389/fmicb.2015.01302/fullDNA Repairprotein-protein interactionDeinococcus radioduransHERADNA end resectionRecJ |
| spellingShingle | Kaiying eCheng Ye eZhao Xuanyi eChen Tao eLi Liangyan eWang Hong eXu Bing eTian Yuejin eHua A novel C-terminal domain of RecJ is critical for interaction with HerA in Deinococcus radiodurans Frontiers in Microbiology DNA Repair protein-protein interaction Deinococcus radiodurans HERA DNA end resection RecJ |
| title | A novel C-terminal domain of RecJ is critical for interaction with HerA in Deinococcus radiodurans |
| title_full | A novel C-terminal domain of RecJ is critical for interaction with HerA in Deinococcus radiodurans |
| title_fullStr | A novel C-terminal domain of RecJ is critical for interaction with HerA in Deinococcus radiodurans |
| title_full_unstemmed | A novel C-terminal domain of RecJ is critical for interaction with HerA in Deinococcus radiodurans |
| title_short | A novel C-terminal domain of RecJ is critical for interaction with HerA in Deinococcus radiodurans |
| title_sort | novel c terminal domain of recj is critical for interaction with hera in deinococcus radiodurans |
| topic | DNA Repair protein-protein interaction Deinococcus radiodurans HERA DNA end resection RecJ |
| url | http://journal.frontiersin.org/Journal/10.3389/fmicb.2015.01302/full |
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