scholarly journals Inventory and Evolution of Mitochondrion-localized Family A DNA Polymerases in Euglenozoa

Pathogens ◽  
2020 ◽  
Vol 9 (4) ◽  
pp. 257 ◽  
Author(s):  
Ryo Harada ◽  
Yoshihisa Hirakawa ◽  
Akinori Yabuki ◽  
Yuichiro Kashiyama ◽  
Moe Maruyama ◽  
...  
Keyword(s):  
Dna Polymerase ◽  
Dna Polymerases ◽  
Dna Polymerase I ◽  
Bacterial Dna ◽  
Polymerase Gamma ◽  
Origin And Evolution ◽  
Dna Polymerase Gamma ◽  
Unique Biology ◽  
Organellar Dna ◽  
Polymerase I

The order Trypanosomatida has been well studied due to its pathogenicity and the unique biology of the mitochondrion. In Trypanosoma brucei, four DNA polymerases, namely PolIA, PolIB, PolIC, and PolID, related to bacterial DNA polymerase I (PolI), were shown to be localized in mitochondria experimentally. These mitochondrion-localized DNA polymerases are phylogenetically distinct from other family A DNA polymerases, such as bacterial PolI, DNA polymerase gamma (Polγ) in human and yeasts, “plant and protist organellar DNA polymerase (POP)” in diverse eukaryotes. However, the diversity of mitochondrion-localized DNA polymerases in Euglenozoa other than Trypanosomatida is poorly understood. In this study, we discovered putative mitochondrion-localized DNA polymerases in broad members of three major classes of Euglenozoa—Kinetoplastea, Diplonemea, and Euglenida—to explore the origin and evolution of trypanosomatid PolIA-D. We unveiled distinct inventories of mitochondrion-localized DNA polymerases in the three classes: (1) PolIA is ubiquitous across the three euglenozoan classes, (2) PolIB, C, and D are restricted in kinetoplastids, (3) new types of mitochondrion-localized DNA polymerases were identified in a prokinetoplastid and diplonemids, and (4) evolutionarily distinct types of POP were found in euglenids. We finally propose scenarios to explain the inventories of mitochondrion-localized DNA polymerases in Kinetoplastea, Diplonemea, and Euglenida.

scholarly journals NtPolI-like1 and NtPolI-like2, Bacterial DNA Polymerase I Homologs Isolated from BY-2 Cultured Tobacco Cells, Encode DNA Polymerases Engaged in DNA Replication in Both Plastids and Mitochondria

2007 ◽  
Vol 48 (12) ◽  
pp. 1679-1692 ◽  
Author(s):  
Y. Ono ◽  
A. Sakai ◽  
K. Takechi ◽  
S. Takio ◽  
M. Takusagawa ◽  
...  
Keyword(s):  
Dna Replication ◽  
Dna Polymerase ◽  
Dna Polymerases ◽  
Dna Polymerase I ◽  
Tobacco Cells ◽  
Bacterial Dna ◽  
Polymerase I

Inhibition by Cyclic Guanosine 3':5'-Monophosphate of the Soluble DNA Polymerase Activity, and of Partially Purified DNA Polymerase A (DNA Polymerase I) from the Yeast Saccharomyces cerevisiae

1981 ◽  
Vol 36 (9-10) ◽  
pp. 813-819 ◽  
Author(s):  
Hans Eckstein
Keyword(s):  
Dna Polymerase ◽  
Dna Polymerases ◽  
Nuclease Activity ◽  
Polymerase Activity ◽  
Yeast Cells ◽  
Primer Binding Site ◽  
Dna Polymerase I ◽  
Yeast Saccharomyces Cerevisiae ◽  
Main Component ◽  
Polymerase I

Abstract Dedicated to Professor Dr. Joachim Kühnau on the Occasion of His 80th Birthday cGMP, DNA Polymerase Activity, DNA Polymerase A, DNA Polymerase I, Baker's Yeast DNA polymerase activity from extracts of growing yeast cells is inhibited by cGMP. Experiments with partially purified yeast DNA polymerases show, that cGMP inhibits DNA polymerase A (DNA polymerase I from Chang), which is the main component of the soluble DNA polymerase activity in yeast extracts, by competing for the enzyme with the primer-template DNA. Since the enzyme is not only inhibited by 3',5'-cGMP, but also by 3',5'-cAMP, the 3': 5'-phosphodiester seems to be crucial for the competition between cGMP and primer. This would be inconsistent with the concept of a 3'-OH primer binding site in the enzyme. The existence of such a site in the yeast DNA polymerase A is indicated from studies with various purine nucleoside monophosphates.When various DNA polymerases are compared, inhibition by cGMP seems to be restricted to those enzymes, which are involved in DNA replication. DNA polymerases with an associated nuclease activity are not inhibited, DNA polymerase B from yeast is even activated by cGMP. Though some relations between the cGMP effect and the presumed function of the enzymes in the living cell are apparent, the biological meaning of the observations in general remains open.

scholarly journals Widespread eukaryotic sequences, highly similar to bacterial DNA polymerase I, looking for functions

1997 ◽  
Vol 7 (8) ◽  
pp. R462-R466 ◽  
Author(s):  
Erik L.L. Sonnhammer ◽  
John C. Wootton
Keyword(s):  
Dna Polymerase ◽  
Dna Polymerase I ◽  
Bacterial Dna ◽  
Polymerase I

Mutability of DNA polymerase I: Implications for the creation of mutant DNA polymerases

DNA Repair ◽  
2005 ◽  
Vol 4 (12) ◽  
pp. 1390-1398 ◽  
Author(s):  
Ern Loh ◽  
Lawrence A. Loeb
Keyword(s):  
Dna Polymerase ◽  
Dna Polymerases ◽  
Dna Polymerase I ◽  
The Creation ◽  
Polymerase I

scholarly journals Polymerization activity of an alpha-like DNA polymerase requires a conserved 3'-5' exonuclease active site

1991 ◽  
Vol 11 (9) ◽  
pp. 4786-4795
Author(s):  
J S Gibbs ◽  
K Weisshart ◽  
P Digard ◽  
A deBruynKops ◽  
D M Knipe ◽  
...  
Keyword(s):  
Dna Polymerase ◽  
Active Site ◽  
Dna Polymerases ◽  
Polymerase Activity ◽  
Cell Nuclei ◽  
Dna Polymerase I ◽  
Viral Dna ◽  
Gene Encoding ◽  
Simplex Virus ◽  
Polymerase I

Most DNA polymerases are multifunctional proteins that possess both polymerizing and exonucleolytic activities. For Escherichia coli DNA polymerase I and its relatives, polymerase and exonuclease activities reside on distinct, separable domains of the same polypeptide. The catalytic subunits of the alpha-like DNA polymerase family share regions of sequence homology with the 3'-5' exonuclease active site of DNA polymerase I; in certain alpha-like DNA polymerases, these regions of homology have been shown to be important for exonuclease activity. This finding has led to the hypothesis that alpha-like DNA polymerases also contain a distinct 3'-5' exonuclease domain. We have introduced conservative substitutions into a 3'-5' exonuclease active site homology in the gene encoding herpes simplex virus DNA polymerase, an alpha-like polymerase. Two mutants were severely impaired for viral DNA replication and polymerase activity. The mutants were not detectably affected in the ability of the polymerase to interact with its accessory protein, UL42, or to colocalize in infected cell nuclei with the major viral DNA-binding protein, ICP8, suggesting that the mutation did not exert global effects on protein folding. The results raise the possibility that there is a fundamental difference between alpha-like DNA polymerases and E. coli DNA polymerase I, with less distinction between 3'-5' exonuclease and polymerase functions in alpha-like DNA polymerases.

Large Fragment of DNA Polymerase I from Geobacillus sp. 777: Cloning and Comparison with DNA Polymerases I in Practical Applications

2015 ◽  
Vol 57 (10) ◽  
pp. 947-959 ◽  
Author(s):  
Igor P. Oscorbin ◽  
Ulyana A. Boyarskikh ◽  
Maksim L. Filipenko
Keyword(s):  
Dna Polymerase ◽  
Dna Polymerases ◽  
Large Fragment ◽  
Dna Polymerase I ◽  
Practical Applications ◽  
Polymerase I

Bacterial DNA Polymerase I

2010 ◽  
Author(s):  
William J Allen ◽  
Ying Li ◽  
Gabriel Waksman
Keyword(s):  
Dna Polymerase ◽  
Dna Polymerase I ◽  
Bacterial Dna ◽  
Polymerase I
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