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Gene Review

KTI11  -  Kti11p

Saccharomyces cerevisiae S288c

Synonyms: DPH3, Diphthamide biosynthesis protein 3, Kluyveromyces lactis toxin-insensitive protein 11, YBL071W-A
 
 
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Disease relevance of KTI11

 

High impact information on KTI11

 

Biological context of KTI11

 

Associations of KTI11 with chemical compounds

  • We present the first experimental evidence that Kti11p can bind a single Zn(2+) ion by its four conserved cysteine residues [3].
 

Other interactions of KTI11

  • Using TAP tagging, Kti11p contacts Elongator and translational proteins (Rps7Ap, Rps19Ap Eft2p, Yil103wp, Dph2p) [2].
 

Analytical, diagnostic and therapeutic context of KTI11

References

  1. KTI11 and KTI13, Saccharomyces cerevisiae genes controlling sensitivity to G1 arrest induced by Kluyveromyces lactis zymocin. Fichtner, L., Schaffrath, R. Mol. Microbiol. (2002) [Pubmed]
  2. Elongator's toxin-target (TOT) function is nuclear localization sequence dependent and suppressed by post-translational modification. Fichtner, L., Jablonowski, D., Schierhorn, A., Kitamoto, H.K., Stark, M.J., Schaffrath, R. Mol. Microbiol. (2003) [Pubmed]
  3. Solution structure of Kti11p from Saccharomyces cerevisiae reveals a novel zinc-binding module. Sun, J., Zhang, J., Wu, F., Xu, C., Li, S., Zhao, W., Wu, Z., Wu, J., Zhou, C.Z., Shi, Y. Biochemistry (2005) [Pubmed]
  4. Dph3, a small protein required for diphthamide biosynthesis, is essential in mouse development. Liu, S., Wiggins, J.F., Sreenath, T., Kulkarni, A.B., Ward, J.M., Leppla, S.H. Mol. Cell. Biol. (2006) [Pubmed]
  5. The yeast elongator histone acetylase requires Sit4-dependent dephosphorylation for toxin-target capacity. Jablonowski, D., Fichtner, L., Stark, M.J., Schaffrath, R. Mol. Biol. Cell (2004) [Pubmed]
 
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