The zinc finger is a protein domain that imparts specific nucleic acid
-binding activity on a wide range of functionally important proteins.
In this paper we report the molecular cloning and characterization of
a novel murine zinc-finger gene, mZ13, Analysis of mZ13 cDNAs revealed
that the gene expresses a 794-amino-acid protein encoded by a 2.7 kb
transcript. The protein has an unusual arrangement of 13 zinc fingers
into a 'hand' of 12 tandem fingers and a single isolated finger near t
he C-terminus, This structural organization is conserved with the prob
able chicken homologue, cZ13. mZ13 also contained an additional domain
at the N-terminus which has previously been implicated in the regulat
ion of zinc-finger transcription factor DNA-binding, via protein-prote
in interactions. mZ13 expression was detected in a wide range of murin
e embryonic and adult tissues. The structural organization of mZ13 and
its expression profile suggest that it may function as a housekeeping
DNA-binding protein that regulates the expression of specific genes.