Worm Breeder's Gazette 11(5): 43

These abstracts should not be cited in bibliographies. Material contained herein should be treated as personal communication and should be cited as such only with the consent of the author.

A Zinc Finger Protein that Binds the unc-54 Enhancer and Promoter

Verena Plunger and Andrew Fire

We have been screening expression libraries for clones encoding 
potential myogenic regulatory factors.  Oligonucleotides covering the 
unc-54 enhancer and promoter segments (see WBG 11#2 p.  23) were 
catenated and radioactively labelled.  These were then used to screen 
plaques from a variety of genomic and cDNA expression libraries (from 
Clonetech, Stratagene and Bob Barstead).  Positive plaques were 
followed by confirming binding to the specific oligonucleotides, and 
by testing for binding to nonspecific oligos.  The only clones to date 
which exhibit strong specificity for myosin control sequences are four 
phage from a Clonetech lambda gt11 cDNA library.  The fusion proteins 
produced by these clones bind to both the internal and upstream 
control regions from unc-54, but do not bind to two other non-specific 
double stranded oligonucleotides or to single stranded DNA.  Three of 
the phage have inserts of about 5 kb and one has an insert of 1.4kb.  
The four clones are identical in the region just 3' to lacZ in lambda 
gt11.  All four phage produce  -gal fusion proteins with identical gel 
mobilities, each containing 32kd of protein encoded by the insert.  
The fusion proteins are unstable in E.  coli.The 1.4kb insert has been 
sequenced and encodes a zinc finger protein, which belongs to the same 
class as the Drosophila Kruppel gene product.