Abstract
We have cloned and characterized a novel zinc finger protein, termed JAZ. JAZ contains four C(2)H(2)-type zinc finger motifs that are connected by long (28-38) amino acid linker sequences. JAZ is expressed in all tissues tested and localizes in the nucleus, primarily the nucleolus. JAZ preferentially binds to double-stranded (ds) RNA or RNA/DNA hybrids rather than DNA. Mutation of individual zinc finger motifs reveals that the zinc finger domains are not only essential for dsRNA binding but are also required for its nucleolar localization, which demonstrates a complex trafficking mechanism dependent on the nucleic acid-binding capability of the protein. Furthermore, forced expression of JAZ potently induces apoptosis in murine fibroblast cells. Thus, JAZ may belong to a class of zinc finger proteins that features dsRNA binding and may regulate cell growth via the unique dsRNA binding properties.
Highlights
Interactions between nucleic acids and proteins are fundamental to many cellular processes
A C2H2-type zinc finger (ZF) protein was cloned by screening a Xenopus ovary cDNA expression library using dsRNA as probe [12]
Our results show that JAZ has a higher affinity for an A-form duplex dsRNA than a B-form duplex DNA, demonstrating that mammalian cells express dsRNA-binding ZF proteins
Summary
Interactions between nucleic acids and proteins are fundamental to many cellular processes. Xenopus dsRBP-ZFa has been characterized as a unique C2H2-type ZF protein that can bind dsRNA and RNA-DNA hybrids [12]. The eluted samples and 50 g of the whole cell lysates were loaded onto a 10% SDS-PAGE gel followed by immunoblotting using an anti-HA antibody (12CA5, Roche Molecular Biochemicals) for HA-JAZ or an anti-GFP antiserum (CLONTECH) for GFP fusion proteins.
Sign-in/Register to view highlights & summary Sign-in/Register to access full text options 
Free) 
Talk to us
Join us for a 30 min session where you can share your feedback and ask us any queries you have
Schedule a call
