Difference between revisions of "YBL071W-A"
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| − | '''Description of YBL071W-A:''' | + | '''Description of YBL071W-A:''' Zn-ribbon protein that co-purifies with Dph1, Dph2, Eft2 and Elongator subunits Iki3p, Elp2p, and Elp3p as a complex required for synthesis of diphthamide, a modified histidine residue, and for modification of wobble nucleosides in tRNA<ref name='S000124746'>Proudfoot M, et al. (2008) Biochemical and structural characterization of a novel family of cystathionine beta-synthase domain proteins fused to a Zn ribbon-like domain. J Mol Biol 375(1):301-15 {{SGDpaper|S000124746}} PMID 18021800</ref><ref name='S000081138'>Huang B, et al. (2005) An early step in wobble uridine tRNA modification requires the Elongator complex. RNA 11(4):424-36 {{SGDpaper|S000081138}} PMID 15769872</ref><ref name='S000079857'>Liu S, et al. (2004) Identification of the proteins required for biosynthesis of diphthamide, the target of bacterial ADP-ribosylating toxins on translation elongation factor 2. Mol Cell Biol 24(21):9487-97 {{SGDpaper|S000079857}} PMID 15485916</ref><ref name='S000074040'>Fichtner L, et al. (2003) Elongator's toxin-target (TOT) function is nuclear localization sequence dependent and suppressed by post-translational modification. Mol Microbiol 49(5):1297-307 {{SGDpaper|S000074040}} PMID 12940988</ref><ref name='S000069896'>Fichtner L and Schaffrath R (2002) KTI11 and KTI13, Saccharomyces cerevisiae genes controlling sensitivity to G1 arrest induced by Kluyveromyces lactis zymocin. Mol Microbiol 44(3):865-75 |
{{SGDpaper|S000069896}} PMID 11994165</ref> | {{SGDpaper|S000069896}} PMID 11994165</ref> | ||
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Revision as of 06:21, 26 February 2009
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| Systematic name | YBL071W-A |
| Gene name | KTI11 |
| Aliases | DPH3 |
| Feature type | ORF, Verified |
| Coordinates | Chr II:89976..90224 |
| Primary SGDID | S000007587 |
Description of YBL071W-A: Zn-ribbon protein that co-purifies with Dph1, Dph2, Eft2 and Elongator subunits Iki3p, Elp2p, and Elp3p as a complex required for synthesis of diphthamide, a modified histidine residue, and for modification of wobble nucleosides in tRNA[1][2][3][4][5]
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References
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- ↑ Proudfoot M, et al. (2008) Biochemical and structural characterization of a novel family of cystathionine beta-synthase domain proteins fused to a Zn ribbon-like domain. J Mol Biol 375(1):301-15 SGD PMID 18021800
- ↑ Huang B, et al. (2005) An early step in wobble uridine tRNA modification requires the Elongator complex. RNA 11(4):424-36 SGD PMID 15769872
- ↑ Liu S, et al. (2004) Identification of the proteins required for biosynthesis of diphthamide, the target of bacterial ADP-ribosylating toxins on translation elongation factor 2. Mol Cell Biol 24(21):9487-97 SGD PMID 15485916
- ↑ Fichtner L, et al. (2003) Elongator's toxin-target (TOT) function is nuclear localization sequence dependent and suppressed by post-translational modification. Mol Microbiol 49(5):1297-307 SGD PMID 12940988
- ↑ Fichtner L and Schaffrath R (2002) KTI11 and KTI13, Saccharomyces cerevisiae genes controlling sensitivity to G1 arrest induced by Kluyveromyces lactis zymocin. Mol Microbiol 44(3):865-75 SGD PMID 11994165
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