Mgm101: A double-duty Rad52-like protein.
Mgm101 has well-characterized activity for the repair and replication of the mitochondrial genome. Recent work has demonstrated a further role for Mgm101 in nuclear DNA metabolism, contributing to an S-phase specific DNA interstrand cross-link repair pathway that acts redundantly with a pathway cont...
| Main Authors: | , , , , , , , |
|---|---|
| Format: | Journal article |
| Language: | English |
| Published: |
Taylor and Francis
2016
|
| _version_ | 1797071587927654400 |
|---|---|
| author | Rendeková, J Ward, T Šimoničová, L Thomas, P Nosek, J Tomáška, Ľ McHugh, P Chovanec, M |
| author_facet | Rendeková, J Ward, T Šimoničová, L Thomas, P Nosek, J Tomáška, Ľ McHugh, P Chovanec, M |
| author_sort | Rendeková, J |
| collection | OXFORD |
| description | Mgm101 has well-characterized activity for the repair and replication of the mitochondrial genome. Recent work has demonstrated a further role for Mgm101 in nuclear DNA metabolism, contributing to an S-phase specific DNA interstrand cross-link repair pathway that acts redundantly with a pathway controlled by Pso2 exonuclease. Due to involvement of FANCM, FANCJ and FANCP homologues (Mph1, Chl1 and Slx4), this pathway has been described as a Fanconi anemia-like pathway. In this pathway, Mgm101 physically interacts with the DNA helicase Mph1 and the MutSα (Msh2/Msh6) heterodimer, but its precise role is yet to be elucidated. Data presented here suggests that Mgm101 functionally overlaps with Rad52, supporting previous suggestions that, based on protein structure and biochemical properties, Mgm101 and Rad52 belong to a family of proteins with similar function. In addition, our data shows that this overlap extends to the function of both proteins at telomeres, where Mgm101 is required for telomere elongation during chromosome replication in rad52 defective cells. We hypothesize that Mgm101 could, in Rad52-like manner, preferentially bind single-stranded DNAs (such as at stalled replication forks, broken chromosomes and natural chromosome ends), stabilize them and mediate single-strand annealing-like homologous recombination event to prevent them from converting into toxic structures. |
| first_indexed | 2024-03-06T22:55:29Z |
| format | Journal article |
| id | oxford-uuid:6037d6c2-fefc-47b6-b933-8307b026cb88 |
| institution | University of Oxford |
| language | English |
| last_indexed | 2024-03-06T22:55:29Z |
| publishDate | 2016 |
| publisher | Taylor and Francis |
| record_format | dspace |
| spelling | oxford-uuid:6037d6c2-fefc-47b6-b933-8307b026cb882022-03-26T17:52:03ZMgm101: A double-duty Rad52-like protein.Journal articlehttp://purl.org/coar/resource_type/c_dcae04bcuuid:6037d6c2-fefc-47b6-b933-8307b026cb88EnglishSymplectic Elements at OxfordTaylor and Francis2016Rendeková, JWard, TŠimoničová, LThomas, PNosek, JTomáška, ĽMcHugh, PChovanec, MMgm101 has well-characterized activity for the repair and replication of the mitochondrial genome. Recent work has demonstrated a further role for Mgm101 in nuclear DNA metabolism, contributing to an S-phase specific DNA interstrand cross-link repair pathway that acts redundantly with a pathway controlled by Pso2 exonuclease. Due to involvement of FANCM, FANCJ and FANCP homologues (Mph1, Chl1 and Slx4), this pathway has been described as a Fanconi anemia-like pathway. In this pathway, Mgm101 physically interacts with the DNA helicase Mph1 and the MutSα (Msh2/Msh6) heterodimer, but its precise role is yet to be elucidated. Data presented here suggests that Mgm101 functionally overlaps with Rad52, supporting previous suggestions that, based on protein structure and biochemical properties, Mgm101 and Rad52 belong to a family of proteins with similar function. In addition, our data shows that this overlap extends to the function of both proteins at telomeres, where Mgm101 is required for telomere elongation during chromosome replication in rad52 defective cells. We hypothesize that Mgm101 could, in Rad52-like manner, preferentially bind single-stranded DNAs (such as at stalled replication forks, broken chromosomes and natural chromosome ends), stabilize them and mediate single-strand annealing-like homologous recombination event to prevent them from converting into toxic structures. |
| spellingShingle | Rendeková, J Ward, T Šimoničová, L Thomas, P Nosek, J Tomáška, Ľ McHugh, P Chovanec, M Mgm101: A double-duty Rad52-like protein. |
| title | Mgm101: A double-duty Rad52-like protein. |
| title_full | Mgm101: A double-duty Rad52-like protein. |
| title_fullStr | Mgm101: A double-duty Rad52-like protein. |
| title_full_unstemmed | Mgm101: A double-duty Rad52-like protein. |
| title_short | Mgm101: A double-duty Rad52-like protein. |
| title_sort | mgm101 a double duty rad52 like protein |
| work_keys_str_mv | AT rendekovaj mgm101adoubledutyrad52likeprotein AT wardt mgm101adoubledutyrad52likeprotein AT simonicoval mgm101adoubledutyrad52likeprotein AT thomasp mgm101adoubledutyrad52likeprotein AT nosekj mgm101adoubledutyrad52likeprotein AT tomaskal mgm101adoubledutyrad52likeprotein AT mchughp mgm101adoubledutyrad52likeprotein AT chovanecm mgm101adoubledutyrad52likeprotein |