Difference between revisions of "YNL246W"
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| − | '''Description of YNL246W:''' NAP family histone chaperone; binds to histones and Rtt109p, stimulating histone acetyltransferase activity; possesses nucleosome assembly activity in vitro; proposed role in vacuolar protein sorting and in double-strand break repair<ref name='S000070264'>Bonangelino CJ, et al. (2002) Genomic screen for vacuolar protein sorting genes in Saccharomyces cerevisiae. Mol Biol Cell 13(7):2486-501 {{SGDpaper|S000070264}} PMID 12134085</ref><ref name=' | + | '''Description of YNL246W:''' NAP family histone chaperone; binds to histones and Rtt109p, stimulating histone acetyltransferase activity; possesses nucleosome assembly activity in vitro; proposed role in vacuolar protein sorting and in double-strand break repair<ref name='S000070264'>Bonangelino CJ, et al. (2002) Genomic screen for vacuolar protein sorting genes in Saccharomyces cerevisiae. Mol Biol Cell 13(7):2486-501 {{SGDpaper|S000070264}} PMID 12134085</ref><ref name='S000126328'>Fillingham J, et al. (2008) Chaperone control of the activity and specificity of the histone H3 acetyltransferase Rtt109. Mol Cell Biol 28(13):4342-53 {{SGDpaper|S000126328}} PMID 18458063</ref><ref name='S000122001'>Han J, et al. (2007) The Rtt109-Vps75 Histone Acetyltransferase Complex Acetylates Non-nucleosomal Histone H3. J Biol Chem 282(19):14158-64 {{SGDpaper|S000122001}} PMID 17369253</ref><ref name='S000124825'>Jessulat M, et al. (2008) Interacting proteins Rtt109 and Vps75 affect the efficiency of non-homologous end-joining in Saccharomyces cerevisiae. Arch Biochem Biophys 469(2):157-64 {{SGDpaper|S000124825}} PMID 18036332</ref><ref name='S000129115'>Park YJ, et al. (2008) Histone chaperone specificity in Rtt109 activation. Nat Struct Mol Biol 15(9):957-64 {{SGDpaper|S000129115}} PMID 19172749</ref><ref name='S000121319'>Selth L and Svejstrup JQ (2007) Vps75, A New Yeast Member of the NAP Histone Chaperone Family. J Biol Chem 282(17):12358-62 |
| − | {{SGDpaper| | + | {{SGDpaper|S000121319}} PMID 17344218</ref> |
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Revision as of 14:05, 25 February 2010
Share your knowledge...Edit this entry! <protect>
| Systematic name | YNL246W |
| Gene name | VPS75 |
| Aliases | |
| Feature type | ORF, Verified |
| Coordinates | Chr XIV:185461..186350 |
| Primary SGDID | S000005190 |
Description of YNL246W: NAP family histone chaperone; binds to histones and Rtt109p, stimulating histone acetyltransferase activity; possesses nucleosome assembly activity in vitro; proposed role in vacuolar protein sorting and in double-strand break repair[1][2][3][4][5][6]
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References
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- ↑ Bonangelino CJ, et al. (2002) Genomic screen for vacuolar protein sorting genes in Saccharomyces cerevisiae. Mol Biol Cell 13(7):2486-501 SGD PMID 12134085
- ↑ Fillingham J, et al. (2008) Chaperone control of the activity and specificity of the histone H3 acetyltransferase Rtt109. Mol Cell Biol 28(13):4342-53 SGD PMID 18458063
- ↑ Han J, et al. (2007) The Rtt109-Vps75 Histone Acetyltransferase Complex Acetylates Non-nucleosomal Histone H3. J Biol Chem 282(19):14158-64 SGD PMID 17369253
- ↑ Jessulat M, et al. (2008) Interacting proteins Rtt109 and Vps75 affect the efficiency of non-homologous end-joining in Saccharomyces cerevisiae. Arch Biochem Biophys 469(2):157-64 SGD PMID 18036332
- ↑ Park YJ, et al. (2008) Histone chaperone specificity in Rtt109 activation. Nat Struct Mol Biol 15(9):957-64 SGD PMID 19172749
- ↑ Selth L and Svejstrup JQ (2007) Vps75, A New Yeast Member of the NAP Histone Chaperone Family. J Biol Chem 282(17):12358-62 SGD PMID 17344218
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