PMID- 10444065
OWN - NLM
STAT- MEDLINE
DCOM- 19990901
LR  - 20191023
IS  - 0021-9525 (Print)
IS  - 0021-9525 (Linking)
VI  - 146
IP  - 3
DP  - 1999 Aug 9
TI  - Localization in the nucleolus and coiled bodies of protein subunits of the
      ribonucleoprotein ribonuclease P.
PG  - 559-72
AB  - The precise location of the tRNA processing ribonucleoprotein ribonuclease P
      (RNase P) and the mechanism of its intranuclear distribution have not been
      completely delineated. We show that three protein subunits of human RNase P
      (Rpp), Rpp14, Rpp29 and Rpp38, are found in the nucleolus and that each can
      localize a reporter protein to nucleoli of cells in tissue culture. In contrast
      to Rpp38, which is uniformly distributed in nucleoli, Rpp14 and Rpp29 are
      confined to the dense fibrillar component. Rpp29 and Rpp38 possess functional,
      yet distinct domains required for subnucleolar localization. The subunit Rpp14
      lacks such a domain and appears to be dependent on a piggyback process to reach
      the nucleolus. Biochemical analysis suggests that catalytically active RNase P
      exists in the nucleolus. We also provide evidence that Rpp29 and Rpp38 reside in 
      coiled bodies, organelles that are implicated in the biogenesis of several other 
      small nuclear ribonucleoproteins required for processing of precursor mRNA.
      Because some protein subunits of RNase P are shared by the ribosomal RNA
      processing ribonucleoprotein RNase MRP, these two evolutionary related
      holoenzymes may share common intranuclear localization and assembly pathways to
      coordinate the processing of tRNA and rRNA precursors.
FAU - Jarrous, N
AU  - Jarrous N
AD  - Department of Molecular, Cellular and Developmental Biology, Yale University, New
      Haven, Connecticut 06520, USA.
FAU - Wolenski, J S
AU  - Wolenski JS
FAU - Wesolowski, D
AU  - Wesolowski D
FAU - Lee, C
AU  - Lee C
FAU - Altman, S
AU  - Altman S
LA  - eng
GR  - GM-19422/GM/NIGMS NIH HHS/United States
PT  - Journal Article
PT  - Research Support, Non-U.S. Gov't
PT  - Research Support, U.S. Gov't, Non-P.H.S.
PT  - Research Support, U.S. Gov't, P.H.S.
PL  - United States
TA  - J Cell Biol
JT  - The Journal of cell biology
JID - 0375356
RN  - 0 (Autoantigens)
RN  - 0 (Holoenzymes)
RN  - 0 (Protein Sorting Signals)
RN  - 0 (RNA Precursors)
RN  - 0 (RNA, Catalytic)
RN  - 0 (RNA, Transfer, Ser)
RN  - 0 (Ribonucleoproteins)
RN  - EC 3.1.- (Endoribonucleases)
RN  - EC 3.1.26.5 (RPP14 protein, human)
RN  - EC 3.1.26.5 (RPP38 protein, human)
RN  - EC 3.1.26.5 (Ribonuclease P)
SB  - IM
MH  - Amino Acid Sequence
MH  - Animals
MH  - Autoantigens/chemistry/genetics/metabolism
MH  - Biological Transport
MH  - Catalysis
MH  - Cell Line
MH  - Cell Nucleolus/*enzymology/genetics
MH  - Endoribonucleases/*chemistry/genetics/*metabolism
MH  - Holoenzymes/chemistry/genetics/metabolism
MH  - Humans
MH  - Mice
MH  - Molecular Sequence Data
MH  - Molecular Weight
MH  - Organelles/*enzymology/genetics
MH  - Protein Sorting Signals/chemistry/genetics/metabolism
MH  - RNA Precursors/genetics
MH  - RNA Processing, Post-Transcriptional
MH  - RNA, Catalytic/*chemistry/genetics/*metabolism
MH  - RNA, Transfer, Ser/genetics
MH  - Ribonuclease P
MH  - Ribonucleoproteins/*chemistry/genetics/*metabolism
MH  - Sequence Deletion
MH  - Transfection
PMC - PMC2150555
EDAT- 1999/08/12 00:00
MHDA- 1999/08/12 00:01
CRDT- 1999/08/12 00:00
PHST- 1999/08/12 00:00 [pubmed]
PHST- 1999/08/12 00:01 [medline]
PHST- 1999/08/12 00:00 [entrez]
AID - 10.1083/jcb.146.3.559 [doi]
PST - ppublish
SO  - J Cell Biol. 1999 Aug 9;146(3):559-72. doi: 10.1083/jcb.146.3.559.