In a screen for myosin-like proteins in embryonic chicken brain, we have identified a novel nuclear protein structurally related to hnRNP-U (heterogeneous nuclear ribonuclear protein U). We have called this protein chURP, for chicken U-related protein. In this screen, chURP was immunoreactive with two myosin antibodies and, in common with the unconventional myosins, bound calmodulin in vitro in both the presence and absence of calcium ions. Determination of 757 amino acids of the chURP sequence revealed that it shares 41% amino acid identity with human and rat hnRNP-U, although chURP and hnRNP-U appear not to be orthologous proteins. ChURP is ubiquitously expressed in the nuclei of all chick tissues and, as one of a growing number of calmodulin-binding proteins to be identified in the nucleus, further highlights the potential of calmodulin as a regulator of nuclear metabolism.Keywords: hnRNP particles; nuclear matrix; calmodulin; hnRNP-U.Protein-coding genes in eukaryotes are transcribed by RNA polymerase II to form nascent transcripts which, because of their wide size distribution and subcellular localization, are known as heterogeneous nuclear (hn)RNAs. As soon as hnRNAs begin to emerge from their genes, they associate cotranscriptionally with a variety of proteins to become heterogeneous nuclear ribonucleoprotein (hnRNP) complexes [1,2]. The macromolecular composition of hnRNP complexes is diverse and includes spliceosomes, which are themselves ribonucleoprotein complexes consisting of a variety of small nuclear (sn)RNAs and associated proteins in the form of snRNPs [3,4]. Those proteins associated with hnRNAs that are not stable components of RNP complexes such as spliceosomes are generally called hnRNP proteins [1,5]. Approximately 20 major hnRNP proteins, designated hnRNP-A1 through -U in order of ascending molecular weight, are typically identified in hnRNP complexes immunopurified from various sources [1,6±10]. The cDNAs for many of these proteins have now been cloned although their functions are not completely understood [1,5,11]. For example, various hnRNP proteins have been demonstrated to possess RNA annealing activity which may be important in both cis and trans interactions during pre-mRNA splicing [12±18], while the same proteins may also be involved in regulating the export of mature mRNAs from the nucleus to the cytoplasm [19±27]. HnRNP proteins therefore appear to have complex functions.Consistent with their proposed roles in vivo, hnRNP proteins have been demonstrated to bind RNA in vitro [1,5,10]. Three distinct RNA-binding domains (RBDs), known as the RNP-CS, KH and RGG box motifs, are represented in the hnRNP proteins, sometimes in combination within one particular polypeptide [28]. For example, hnRNP-A1 contains two RNP-CS motifs and one RGG box. The RNA-binding activity of recombinant hnRNP-U has been mapped to a 26-amino-acid RGG box motif in a C-terminal 112 amino acid domain termed U-gly, as it is rich in glycine residues [29]. Interestingly, hnRNP-U has also been independently charact...