Difference between revisions of "YDL164C"
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| − | |valign="top" nowrap bgcolor="{{SGDblue}}"| '''Systematic name''' || [http:// | + | |valign="top" nowrap bgcolor="{{SGDblue}}"| '''Systematic name''' || [http://www.yeastgenome.org/cgi-bin/locus.pl?dbid=S000002323 YDL164C] |
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|valign="top" nowrap bgcolor="{{SGDblue}}"| '''Gene name''' ||''CDC9 '' | |valign="top" nowrap bgcolor="{{SGDblue}}"| '''Gene name''' ||''CDC9 '' | ||
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|valign="top" nowrap bgcolor="{{SGDblue}}"| '''Coordinates''' | |valign="top" nowrap bgcolor="{{SGDblue}}"| '''Coordinates''' | ||
| − | |nowrap| Chr IV: | + | |nowrap| Chr IV:167254..164987 |
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| − | | | + | |valign="top" nowrap bgcolor="{{SGDblue}}"| '''Primary SGDID''' || S000002323 |
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| − | '''Description of | + | '''Description of YDL164C:''' DNA ligase found in the nucleus and mitochondria, an essential enzyme that joins Okazaki fragments during DNA replication; also acts in nucleotide excision repair, base excision repair, and recombination<ref name='S000045500'>Johnston LH and Nasmyth KA (1978) Saccharomyces cerevisiae cell cycle mutant cdc9 is defective in DNA ligase. Nature 274(5674):891-3 {{SGDpaper|S000045500}} PMID 355897</ref><ref name='S000060892'>Lindahl T and Barnes DE (1992) Mammalian DNA ligases. Annu Rev Biochem 61:251-81 {{SGDpaper|S000060892}} PMID 1497311</ref><ref name='S000058459'>Waga S and Stillman B (1998) The DNA replication fork in eukaryotic cells. Annu Rev Biochem 67:721-51 {{SGDpaper|S000058459}} PMID 9759502</ref><ref name='S000043286'>Willer M, et al. (1999) The yeast CDC9 gene encodes both a nuclear and a mitochondrial form of DNA ligase I. Curr Biol 9(19):1085-94 {{SGDpaper|S000043286}} PMID 10531002</ref><ref name='S000046630'>Wu X, et al. (1999) DNA ligation during excision repair in yeast cell-free extracts is specifically catalyzed by the CDC9 gene product. Biochemistry 38(9):2628-35 {{SGDpaper|S000046630}} PMID 10052932</ref><ref name='S000040324'>Zou H and Rothstein R (1997) Holliday junctions accumulate in replication mutants via a RecA homolog-independent mechanism. Cell 90(1):87-96 |
{{SGDpaper|S000040324}} PMID 9230305</ref> | {{SGDpaper|S000040324}} PMID 9230305</ref> | ||
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==Community Commentary== | ==Community Commentary== | ||
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| + | Specifically higher expression in carbon limited chemostat cultures versus carbon excess. | ||
| + | <ref>Boer VM, et al. (2003) The genome-wide transcriptional responses of Saccharomyces cerevisiae grown on glucose in aerobic chemostat cultures limited for carbon, nitrogen, phosphorus, or sulfur. | ||
| + | J Biol Chem 278(5):3265-74</ref> | ||
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==References== | ==References== | ||
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Latest revision as of 07:45, 23 January 2012
Share your knowledge...Edit this entry! <protect>
| Systematic name | YDL164C |
| Gene name | CDC9 |
| Aliases | MMS8 |
| Feature type | ORF, Verified |
| Coordinates | Chr IV:167254..164987 |
| Primary SGDID | S000002323 |
Description of YDL164C: DNA ligase found in the nucleus and mitochondria, an essential enzyme that joins Okazaki fragments during DNA replication; also acts in nucleotide excision repair, base excision repair, and recombination[1][2][3][4][5][6]
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Contents
Community Commentary
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References
See Help:References on how to add references
- ↑ Johnston LH and Nasmyth KA (1978) Saccharomyces cerevisiae cell cycle mutant cdc9 is defective in DNA ligase. Nature 274(5674):891-3 SGD PMID 355897
- ↑ Lindahl T and Barnes DE (1992) Mammalian DNA ligases. Annu Rev Biochem 61:251-81 SGD PMID 1497311
- ↑ Waga S and Stillman B (1998) The DNA replication fork in eukaryotic cells. Annu Rev Biochem 67:721-51 SGD PMID 9759502
- ↑ Willer M, et al. (1999) The yeast CDC9 gene encodes both a nuclear and a mitochondrial form of DNA ligase I. Curr Biol 9(19):1085-94 SGD PMID 10531002
- ↑ Wu X, et al. (1999) DNA ligation during excision repair in yeast cell-free extracts is specifically catalyzed by the CDC9 gene product. Biochemistry 38(9):2628-35 SGD PMID 10052932
- ↑ Zou H and Rothstein R (1997) Holliday junctions accumulate in replication mutants via a RecA homolog-independent mechanism. Cell 90(1):87-96 SGD PMID 9230305
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