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Gene Review:

CDD - cytidine deaminase

Gallus gallus

Kimitsuki, T. et al., Vita, A. et al., Saribasak, H. et al., Conlon, T.M. et al., Arakawa, H. et al., et al.

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High impact information on CDD

Ig gene conversion is most likely initiated by activation-induced cytidine deaminase-mediated cytosine deamination [1].
This suggests that hypermutating B cells process activation-induced cytidine deaminase-induced uracils with approximately one-seventh of uracils giving rise to mutations depending on their position [1].
Rabbit REPR is analogous to a rat enterocyte 27-kDa protein that has been shown to have cytidine deaminase activity [2].
Conversely, overexpression of avian E47, a bHLH transcription factor, leads to a dramatic increase in GC rates independent of IgL or activation-induced cytidine deaminase RNA levels [3].
The effects of cisplatin (cis-dichlorodiammine platinum II, CDDP) on the mechano-electrical transduction (MET) current were investigated with a whole-cell patch-electrode voltage clamp technique in dissociated cochlear hair cells of chicks [4].

Biological context of CDD

The kinetics of CDDP blockade consist of a voltage-independent and a voltage-dependent component [4].
Activation-induced cytidine deaminase initiates immunoglobulin gene conversion and hypermutation by a common intermediate [5].

Associations of CDD with chemical compounds

These findings suggest that a single DHSM molecule or more than one CDDP molecule binds to a single MET channel [6].

Analytical, diagnostic and therapeutic context of CDD

Cytidine deaminase (cytidine aminohydrolase, EC 3.5.4.5) from chicken liver has been obtained in pure form through a rapid procedure consisting of organic solvent precipitation, heat treatment, anionic-exchange chromatography, hydrophobic interaction chromatography followed by two rapid chromatographies using an FPLC system [7].

References

Uracil DNA glycosylase disruption blocks Ig gene conversion and induces transition mutations. Saribasak, H., Saribasak, N.N., Ipek, F.M., Ellwart, J.W., Arakawa, H., Buerstedde, J.M. J. Immunol. (2006) [Pubmed]
Cloning and mutagenesis of the rabbit ApoB mRNA editing protein. A zinc motif is essential for catalytic activity, and noncatalytic auxiliary factor(s) of the editing complex are widely distributed. Yamanaka, S., Poksay, K.S., Balestra, M.E., Zeng, G.Q., Innerarity, T.L. J. Biol. Chem. (1994) [Pubmed]
The chicken Ig light chain 3'-enhancer is essential for gene expression and regulates gene conversion via the transcription factor E2A. Conlon, T.M., Meyer, K.B. Eur. J. Immunol. (2006) [Pubmed]
Cisplatin blocks mechano-electric transducer current in chick cochlear hair cells. Kimitsuki, T., Nakagawa, T., Hisashi, K., Komune, S., Komiyama, S. Hear. Res. (1993) [Pubmed]
Activation-induced cytidine deaminase initiates immunoglobulin gene conversion and hypermutation by a common intermediate. Arakawa, H., Saribasak, H., Buerstedde, J.M. PLoS Biol. (2004) [Pubmed]
The effects of ototoxic drugs on mechano-electric transduction channels in chick cochlear hair cells. Kimitsuki, T., Nakagawa, T., Hisashi, K., Komune, S., Uemura, T. European archives of oto-rhino-laryngology : official journal of the European Federation of Oto-Rhino-Laryngological Societies (EUFOS) : affiliated with the German Society for Oto-Rhino-Laryngology - Head and Neck Surgery. (1994) [Pubmed]
Purification of cytidine deaminase from chicken liver. Vita, A., Cacciamani, T., Natalini, P., Ruggieri, S., Santarelli, I., Magni, G. Ital. J. Biochem. (1987) [Pubmed]

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