title: The hrp23 protein in the balbiani ring pre-mRNP particles is released just before or at the binding of the particles to the nuclear pore complex.
abstract: Balbiani ring (BR) pre-mRNP particles reside in the nuclei of salivary glands of the dipteran Chironomus tentans and carry the message for giant-sized salivary proteins. In the present study, we identify and characterize a new protein component in the BR ribonucleoprotein (RNP) particles, designated hrp23. The protein with a molecular mass of 20 kD has a single RNA-binding domain and a glycine-arginine-serine-rich auxiliary domain. As shown by immunoelectron microscopy, the hrp23 protein is added to the BR transcript concomitant with transcription, is still present in the BR particles in the nucleoplasm, but is absent from the BR particles that are bound to the nuclear pore complex or are translocating through the central channel of the complex. Thus, hrp23 is released just before or at the binding of the particles to the nuclear pore complex. It is noted that hrp23 behaves differently from two other BR RNP proteins earlier studied: hrp36 and hrp45. These proteins both reach the nuclear pore complex, and hrp36 even accompanies the RNA into the cytoplasm. It is concluded that each BR RNA-binding protein seems to have a specific flow pattern, probably related to the particular role of the protein in gene expression.
authors.affiliation: Department of Cell and Molecular Biology, Medical Nobel Institute, Karolinska Institutet, S-171 77, Stockholm, Sweden.
authors.forename: X
authors.initials: X
authors.lastname: Sun
authors.forename: A T
authors.initials: AT
authors.lastname: Alzhanova-Ericsson
authors.forename: N
authors.initials: N
authors.lastname: Visa
authors.forename: Y
authors.initials: Y
authors.lastname: Aissouni
authors.forename: J
authors.initials: J
authors.lastname: Zhao
authors.forename: B
authors.initials: B
authors.lastname: Daneholt
mesh_terms: D000595:Amino Acid Sequence; D000818:Animals; D001483:Base Sequence; D001692:Biological Transport / Q000502:physiology; D002478:Cells, Cultured; D002683:Chironomidae / Q000502:physiology*; D003001:Cloning, Molecular; D034441:Heterogeneous-Nuclear Ribonucleoproteins; D007150:Immunohistochemistry; D019476:Insect Proteins / Q000737:chemistry; D016253:Microscopy, Immunoelectron; D008969:Molecular Sequence Data; D009685:Nuclear Envelope / Q000502:physiology; D009687:Nuclear Proteins / Q000737:chemistry; D012333:RNA, Messenger / Q000235:genetics; D016601:RNA-Binding Proteins / Q000737:chemistry*; D012261:Ribonucleoproteins / Q000737:chemistry*; D012471:Salivary Proteins and Peptides / Q000737:chemistry*; D017422:Sequence Analysis, DNA; D014158:Transcription, Genetic / Q000235:genetics
chemical_list: D034441:Heterogeneous-Nuclear Ribonucleoproteins; D019476:Insect Proteins; D009687:Nuclear Proteins; D012333:RNA, Messenger; D016601:RNA-Binding Proteins; D012261:Ribonucleoproteins; D012471:Salivary Proteins and Peptides; C114860:hrp23 protein, Chironomus tentans