TableEdit

Lodge, AP, Walsh, A, McNamee, CJ and Moss, DJ (1999) Identification of chURP, a nuclear calmodulin-binding protein related to hnRNP-U. Eur. J. Biochem. 261:137-47

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.

PubMed

Alternative Splicing; Amino Acid Sequence; Animals; Base Sequence; Calmodulin-Binding Proteins/genetics; Calmodulin-Binding Proteins/isolation & purification; Calmodulin-Binding Proteins/metabolism; Chickens; DNA Primers/genetics; DNA, Complementary/genetics; Heterogeneous-Nuclear Ribonucleoprotein U; Heterogeneous-Nuclear Ribonucleoproteins; Humans; Molecular Sequence Data; Nuclear Proteins/genetics; Nuclear Proteins/isolation & purification; Nuclear Proteins/metabolism; Rats; Recombinant Fusion Proteins/isolation & purification; Ribonucleoproteins/genetics; Ribonucleoproteins/isolation & purification; Ribonucleoproteins/metabolism; Sequence Homology, Amino Acid