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.

Amino and carboxy-terminal extensions of yeast mitochondrial DNA polymerase assemble both the polymerization and exonuclease active sites / Trasvina-Arenas, C. H.; Hoyos-Gonzalez, N.; Castro-Lara, A. Y.; Rodriguez-Hernandez, A.; Sanchez-Sandoval, M. E.; Jimenez-Sandoval, P.; Ayala-Garcia, V. M.; Diaz-Quezada, C.; Lodi, T.; Baruffini, E.; Brieba, L. G.. - In: MITOCHONDRION. - ISSN 1567-7249. - 49(2019), pp. 166-177. [10.1016/j.mito.2019.08.005]

Amino and carboxy-terminal extensions of yeast mitochondrial DNA polymerase assemble both the polymerization and exonuclease active sites

Lodi T.
Investigation
;
Baruffini E.
Investigation
;
2019

Abstract

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.
Amino and carboxy-terminal extensions of yeast mitochondrial DNA polymerase assemble both the polymerization and exonuclease active sites / Trasvina-Arenas, C. H.; Hoyos-Gonzalez, N.; Castro-Lara, A. Y.; Rodriguez-Hernandez, A.; Sanchez-Sandoval, M. E.; Jimenez-Sandoval, P.; Ayala-Garcia, V. M.; Diaz-Quezada, C.; Lodi, T.; Baruffini, E.; Brieba, L. G.. - In: MITOCHONDRION. - ISSN 1567-7249. - 49(2019), pp. 166-177. [10.1016/j.mito.2019.08.005]
File in questo prodotto:
Non ci sono file associati a questo prodotto.

I documenti in IRIS sono protetti da copyright e tutti i diritti sono riservati, salvo diversa indicazione.

Utilizza questo identificativo per citare o creare un link a questo documento: http://hdl.handle.net/11381/2863042
Citazioni
  • ???jsp.display-item.citation.pmc??? ND
  • Scopus 4
  • ???jsp.display-item.citation.isi??? 4
social impact