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- W2016598731 endingPage "1193" @default.
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- W2016598731 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." @default.
- W2016598731 created "2016-06-24" @default.
- W2016598731 creator A5015694942 @default.
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- W2016598731 creator A5076707975 @default.
- W2016598731 creator A5081366275 @default.
- W2016598731 date "1998-09-07" @default.
- W2016598731 modified "2023-10-01" @default.
- W2016598731 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" @default.
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- W2016598731 doi "https://doi.org/10.1083/jcb.142.5.1181" @default.
- W2016598731 hasPubMedCentralId "https://www.ncbi.nlm.nih.gov/pmc/articles/2149341" @default.
- W2016598731 hasPubMedId "https://pubmed.ncbi.nlm.nih.gov/9732280" @default.
- W2016598731 hasPublicationYear "1998" @default.
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