A. Napier et al., Characterization of the chicken transitin gene reveals a strong relationship to the nestin intermediate filament class, J MOL NEURO, 12(1), 1999, pp. 11-22
Our laboratory previously reported that transitin is a radial glial interme
diate filament protein sharing the basic structural features common to all
intermediate filament (IF) proteins. It contains an a-helical core domain f
lanked by a short nonhelical head and a long COOH-terminal tail. The core s
equence of transitin shows the greatest similarity to Xenopus tanabin and t
o rat and human nestin. We also reported that transitin has multiple splice
variants derived from the deletion or inclusion of a leucine-zipper heptad
repeat domain in the COOH-terminal tail. In the present study, we provide
new evidence to support the classification of nestin and transitin in the s
ame group of IF proteins based on the number and position of its introns. I
n addition, we suggest that the different isoforms of transitin are produce
d by a splicing mechanism that recognizes consensus 5' and 3' splice sites
contained within the coding sequence of the leucine-zipper heptad repeat do
main.