Abstract
In higher eukaryotes, DNA polymerase (pol) beta resides in the nucleus and participates primarily in DNA repair. The DNA polymerase beta from the trypanosomatid Crithidia fasciculata, however, was the first mitochondrial enzyme of this type described. Upon searching the nearly completed genome data base of the related parasite Trypanosoma brucei, we discovered genes for two pol beta-like proteins. One is approximately 70% identical to the C. fasciculata pol beta and is likely the homolog of this enzyme. The other, although approximately 30% identical within the polymerase region, has unusual structural features including a short C-terminal tail and a long N-terminal extension rich in prolines, alanines, and lysines. Both proteins, when expressed recombinantly, are active as DNA polymerases and deoxyribose phosphate lyases, but their polymerase activity optima differ with respect to pH and KCl and MgCl2 concentrations. Remarkably, green fluorescent protein fusion proteins and immunofluorescence demonstrate that both are mitochondrial, but their locations with respect to the mitochondrial DNA (kinetoplast DNA network) in this organism are strikingly different.
| Original language | English (US) |
|---|---|
| Pages (from-to) | 49095-49101 |
| Number of pages | 7 |
| Journal | Journal of Biological Chemistry |
| Volume | 278 |
| Issue number | 49 |
| State | Published - Dec 5 2003 |
Fingerprint
ASJC Scopus subject areas
- Biochemistry
Cite this
Trypanosoma brucei has two distinct mitochondrial DNA polymerase beta enzymes. / Saxowsky, Tina T.; Choudhary, Gunjan; Klingbeil, Michele M.; Englund, Paul T.
In: Journal of Biological Chemistry, Vol. 278, No. 49, 05.12.2003, p. 49095-49101.Research output: Contribution to journal › Article
}
TY - JOUR
T1 - Trypanosoma brucei has two distinct mitochondrial DNA polymerase beta enzymes.
AU - Saxowsky, Tina T.
AU - Choudhary, Gunjan
AU - Klingbeil, Michele M.
AU - Englund, Paul T.
PY - 2003/12/5
Y1 - 2003/12/5
N2 - In higher eukaryotes, DNA polymerase (pol) beta resides in the nucleus and participates primarily in DNA repair. The DNA polymerase beta from the trypanosomatid Crithidia fasciculata, however, was the first mitochondrial enzyme of this type described. Upon searching the nearly completed genome data base of the related parasite Trypanosoma brucei, we discovered genes for two pol beta-like proteins. One is approximately 70% identical to the C. fasciculata pol beta and is likely the homolog of this enzyme. The other, although approximately 30% identical within the polymerase region, has unusual structural features including a short C-terminal tail and a long N-terminal extension rich in prolines, alanines, and lysines. Both proteins, when expressed recombinantly, are active as DNA polymerases and deoxyribose phosphate lyases, but their polymerase activity optima differ with respect to pH and KCl and MgCl2 concentrations. Remarkably, green fluorescent protein fusion proteins and immunofluorescence demonstrate that both are mitochondrial, but their locations with respect to the mitochondrial DNA (kinetoplast DNA network) in this organism are strikingly different.
AB - In higher eukaryotes, DNA polymerase (pol) beta resides in the nucleus and participates primarily in DNA repair. The DNA polymerase beta from the trypanosomatid Crithidia fasciculata, however, was the first mitochondrial enzyme of this type described. Upon searching the nearly completed genome data base of the related parasite Trypanosoma brucei, we discovered genes for two pol beta-like proteins. One is approximately 70% identical to the C. fasciculata pol beta and is likely the homolog of this enzyme. The other, although approximately 30% identical within the polymerase region, has unusual structural features including a short C-terminal tail and a long N-terminal extension rich in prolines, alanines, and lysines. Both proteins, when expressed recombinantly, are active as DNA polymerases and deoxyribose phosphate lyases, but their polymerase activity optima differ with respect to pH and KCl and MgCl2 concentrations. Remarkably, green fluorescent protein fusion proteins and immunofluorescence demonstrate that both are mitochondrial, but their locations with respect to the mitochondrial DNA (kinetoplast DNA network) in this organism are strikingly different.
UR - http://www.scopus.com/inward/record.url?scp=1542677269&partnerID=8YFLogxK
UR - http://www.scopus.com/inward/citedby.url?scp=1542677269&partnerID=8YFLogxK
M3 - Article
C2 - 12966090
AN - SCOPUS:1542677269
VL - 278
SP - 49095
EP - 49101
JO - Journal of Biological Chemistry
JF - Journal of Biological Chemistry
SN - 0021-9258
IS - 49
ER -