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Amino and carboxy-t...
Amino and carboxy-terminal extensions of yeast mitochondrial DNA polymerase assemble both the polymerization and exonuclease active sites
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Trasviña-Arenas, Carlos H. (författare)
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Hoyos-Gonzalez, Nallely (författare)
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Castro-Lara, Atzimba Y. (författare)
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Rodriguez-Hernandez, Annia (författare)
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- Sanchez Sandoval, Maria Eugenia, 1985 (författare)
- Gothenburg University,Göteborgs universitet,Core Facilities, Bioinformatics,Core Facilities, Bioinformatics
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Jimenez-Sandoval, Pedro (författare)
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Ayala-García, Víctor M. (författare)
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Díaz-Quezada, Corina (författare)
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Lodi, Tiziana (författare)
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Baruffini, Enrico (författare)
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Brieba, Luis G. (författare)
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(creator_code:org_t)
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- Elsevier BV, 2019
- 2019
- Engelska.
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Ingår i: Mitochondrion. - : Elsevier BV. - 1567-7249 .- 1872-8278. ; 49, s. 166-177
- Relaterad länk:
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https://doi.org/10.1...
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https://gup.ub.gu.se...
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https://doi.org/10.1...
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Abstract
Ämnesord
Stäng
- Human and yeast mitochondrial DNA polymerases (DNAPs), POLG and Mip1, are related by evolution to bacteriophage DNAPs. However, mitochondrial DNAPs contain unique amino and carboxyl-terminal extensions that physically interact. Here we describe that N-terminal deletions in Mip1 polymerases abolish polymerization and decrease exonucleolytic degradation, whereas moderate C-terminal deletions reduce polymerization. Similarly, to the N-terminal deletions, an extended C-terminal deletion of 298 amino acids is deficient in nucleotide addition and exonucleolytic degradation of double and single-stranded DNA. The latter observation suggests that the physical interaction between the amino and carboxyl-terminal regions of Mip1 may be related to the spread of pathogenic POLG mutant along its primary sequence.
Nyckelord
- DNA polymerase
- DNA replication
- Enzyme kinetics
- Mitochondria
- Regulation
- Structure-function
Publikations- och innehållstyp
- ref (ämneskategori)
- art (ämneskategori)
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