PMID- 9880328
OWN - NLM
STAT- MEDLINE
DCOM- 19990304
LR  - 20231213
IS  - 1059-1524 (Print)
IS  - 1059-1524 (Linking)
VI  - 10
IP  - 1
DP  - 1999 Jan
TI  - Association of nonribosomal nucleolar proteins in ribonucleoprotein complexes 
      during interphase and mitosis.
PG  - 77-90
AB  - rRNA precursors are bound throughout their length by specific proteins, as the 
      pre-rRNAs emerge from the transcription machinery. The association of pre-rRNA 
      with proteins as ribonucleoprotein (RNP) complexes persists during maturation of 
      18S, 5.8S, and 28S rRNA, and through assembly of ribosomal subunits in the 
      nucleolus. Preribosomal RNP complexes contain, in addition to ribosomal proteins, 
      an unknown number of nonribosomal nucleolar proteins, as well as small nucleolar 
      RNA-ribonucleoproteins (sno-RNPs). This report describes the use of a specific, 
      rapid, and mild immunopurification approach to isolate and analyze human RNP 
      complexes that contain nonribosomal nucleolar proteins, as well as ribosomal 
      proteins and rRNA. Complexes immunopurified with antibodies to nucleolin-a major 
      nucleolar RNA-binding protein-contain several distinct specific polypeptides that 
      include, in addition to nucleolin, the previously identified nucleolar proteins 
      B23 and fibrillarin, proteins with electrophoretic mobilities characteristic of 
      ribosomal proteins including ribosomal protein S6, and a number of additional 
      unidentified proteins. The physical association of these proteins with one 
      another is mediated largely by RNA, in that the complexes dissociate upon 
      digestion with RNase. Complexes isolated from M-phase cells are similar in 
      protein composition to those isolated from interphase cell nuclear extracts. 
      Therefore, the predominant proteins that associate with nucleolin in interphase 
      remain in RNP complexes during mitosis, despite the cessation of rRNA synthesis 
      and processing in M-phase. In addition, precursor rRNA, as well as processed 18S 
      and 28S rRNA and candidate rRNA processing intermediates, is found associated 
      with the immunopurified complexes. The characteristics of the rRNP complexes 
      described here, therefore, indicate that they represent bona fide precursors of 
      mature cytoplasmic ribosomal subunits.
FAU - Pinol-Roma, S
AU  - Pinol-Roma S
AD  - Department of Cell Biology and Anatomy, Mount Sinai School of Medicine, New York, 
      New York 10029-6574, USA.
LA  - eng
PT  - Journal Article
PT  - Research Support, U.S. Gov't, P.H.S.
PL  - United States
TA  - Mol Biol Cell
JT  - Molecular biology of the cell
JID - 9201390
RN  - 0 (Chromosomal Proteins, Non-Histone)
RN  - 0 (DNA Probes)
RN  - 0 (Macromolecular Substances)
RN  - 0 (Npm1 protein, mouse)
RN  - 0 (Nuclear Proteins)
RN  - 0 (Phosphoproteins)
RN  - 0 (RNA Precursors)
RN  - 0 (RNA-Binding Proteins)
RN  - 0 (Ribonucleoproteins)
RN  - 0 (Ribosomal Protein S6)
RN  - 0 (Ribosomal Proteins)
RN  - 0 (fibrillarin)
RN  - 117896-08-9 (Nucleophosmin)
SB  - IM
MH  - Animals
MH  - Base Sequence
MH  - Chromosomal Proteins, Non-Histone/isolation & purification/metabolism
MH  - DNA Probes/genetics
MH  - HeLa Cells
MH  - Humans
MH  - Immunohistochemistry
MH  - Interphase/*physiology
MH  - Macromolecular Substances
MH  - Mice
MH  - Mitosis/*physiology
MH  - Nuclear Proteins/isolation & purification/*metabolism
MH  - Nucleophosmin
MH  - Phosphoproteins/isolation & purification/metabolism
MH  - RNA Precursors/genetics/isolation & purification/metabolism
MH  - RNA-Binding Proteins/isolation & purification/metabolism
MH  - Ribonucleoproteins/isolation & purification/*metabolism
MH  - Ribosomal Protein S6
MH  - Ribosomal Proteins/isolation & purification/metabolism
MH  - Ribosomes/chemistry/metabolism
MH  - Nucleolin
PMC - PMC25155
EDAT- 1999/01/08 00:00
MHDA- 1999/01/08 00:01
CRDT- 1999/01/08 00:00
PHST- 1999/01/08 00:00 [pubmed]
PHST- 1999/01/08 00:01 [medline]
PHST- 1999/01/08 00:00 [entrez]
AID - 0766 [pii]
AID - 10.1091/mbc.10.1.77 [doi]
PST - ppublish
SO  - Mol Biol Cell. 1999 Jan;10(1):77-90. doi: 10.1091/mbc.10.1.77.