The protein C4SR contains two cysteine(4) (C(4)) zinc-finger motifs at its amino terminus, a stretch of acidic residues in the middle and a series of serine-arginine (SR) repeats at its carboxyl terminus. A cDNA clone encoding the zinc-finger domain was first selected from a Xenopus laevis oocyte expression library on the basis of the ability of the fusion protein to stably bind an RNA probe. The mRNA encoding C4SR is expressed during oogenesis, and the protein is present at a constant level in oocytes and early embryos. The C4SR protein is expressed in transcriptionally active erythroblasts but not in transcriptionally inert mature erythrocytes. An epitope-tagged C4SR protein, expressed in oocytes, associates with nascent transcripts at many loci in lampbrush chromosomes and is absent from storage particles (snurposomes) containing the normally recognized complement of RNA splicing components. It is likely that C4SR is involved in pre-mRNA transcription/packaging rather than in exon splicing. The zinc-finger motif, present as two copies in C4SR, is also present in a range of transcription-associated proteins. We suggest the descriptor (DW)C(4), in which DW refers to the invariant aspartic acid (D)/tryptophan (W) dipeptide that precedes the first cysteine residue, for this distinctive zinc-finger structure.