PMID- 10618370
OWN - NLM
STAT- MEDLINE
DCOM- 20000210
LR  - 20190501
IS  - 0027-8424 (Print)
IS  - 0027-8424 (Linking)
VI  - 97
IP  - 1
DP  - 2000 Jan 4
TI  - Signal recognition particle components in the nucleolus.
PG  - 55-60
AB  - The signal recognition particle (SRP) is a ribonucleoprotein composed of an Alu
      domain and an S domain. The S domain contains unique sequence SRP RNA and four
      SRP proteins: SRP19, SRP54, SRP68, and SRP72. SRP interacts with ribosomes to
      bring translating membrane and secreted proteins to the endoplasmic reticulum
      (ER) for proper processing. Additionally, SRP RNA is a member of a family of
      small nonribosomal RNAs found recently in the nucleolus, suggesting that the
      nucleolus is more plurifunctional than previously realized. It was therefore of
      interest to determine whether other SRP components localize to this intranuclear 
      site. In transfected rat fibroblasts, green fluorescent protein fusions of SRP19,
      SRP68, and SRP72 localized to the nucleolus, as well as to the cytoplasm, as
      expected. SRP68 also accumulated in the ER, consistent with its affinity for the 
      ER-bound SRP receptor. SRP54 was detected in the cytoplasm as a green fluorescent
      protein fusion and in immunofluorescence studies, but was not detected in the
      nucleolus. In situ hybridization experiments also revealed endogenous SRP RNA in 
      the nucleolus. These results demonstrate that SRP RNA and three SRP proteins
      visit the nucleolus, suggesting that partial SRP assembly, or another
      unidentified activity of the SRP components, occurs at the nucleolus. SRP54
      apparently interacts with nascent SRP beyond the nucleolus, consistent with in
      vitro reconstitution experiments showing that SRP19 must bind to SRP RNA before
      SRP54 binds. Our findings support the notion that the nucleolus is the site of
      assembly and/or interaction between the family of ribonucleoproteins involved in 
      protein synthesis, in addition to ribosomes themselves.
FAU - Politz, J C
AU  - Politz JC
AD  - Department of Biochemistry, University of Massachusetts Medical School, 377
      Plantation Street, Suite 337, Worcester, MA 01605, USA.
FAU - Yarovoi, S
AU  - Yarovoi S
FAU - Kilroy, S M
AU  - Kilroy SM
FAU - Gowda, K
AU  - Gowda K
FAU - Zwieb, C
AU  - Zwieb C
FAU - Pederson, T
AU  - Pederson T
LA  - eng
SI  - GENBANK/AF077109
SI  - GENBANK/AF195951
GR  - R01 GM049034/GM/NIGMS NIH HHS/United States
GR  - GM-21595-23/GM/NIGMS NIH HHS/United States
GR  - F32 AR008361/AR/NIAMS NIH HHS/United States
GR  - AR-08361/AR/NIAMS NIH HHS/United States
GR  - GM-49034/GM/NIGMS NIH HHS/United States
PT  - Journal Article
PT  - Research Support, U.S. Gov't, P.H.S.
PL  - United States
TA  - Proc Natl Acad Sci U S A
JT  - Proceedings of the National Academy of Sciences of the United States of America
JID - 7505876
RN  - 0 (Luminescent Proteins)
RN  - 0 (RNA, Nuclear)
RN  - 0 (Recombinant Fusion Proteins)
RN  - 0 (SRP19 protein, human)
RN  - 0 (SRP54 protein, S cerevisiae)
RN  - 0 (SRP68 protein, S cerevisiae)
RN  - 0 (SRP72 protein, S cerevisiae)
RN  - 0 (SRP72 protein, human)
RN  - 0 (Saccharomyces cerevisiae Proteins)
RN  - 0 (Signal Recognition Particle)
RN  - 147336-22-9 (Green Fluorescent Proteins)
SB  - IM
MH  - Animals
MH  - Cell Line
MH  - Cell Nucleolus/*metabolism
MH  - Endoplasmic Reticulum/metabolism
MH  - Fluorescent Antibody Technique
MH  - Green Fluorescent Proteins
MH  - Humans
MH  - In Situ Hybridization
MH  - Luminescent Proteins
MH  - Molecular Sequence Data
MH  - RNA, Nuclear/metabolism
MH  - Rats
MH  - Recombinant Fusion Proteins
MH  - *Saccharomyces cerevisiae Proteins
MH  - Signal Recognition Particle/*metabolism
MH  - Transfection
PMC - PMC26615
EDAT- 2000/01/05 00:00
MHDA- 2000/01/05 00:01
CRDT- 2000/01/05 00:00
PHST- 2000/01/05 00:00 [pubmed]
PHST- 2000/01/05 00:01 [medline]
PHST- 2000/01/05 00:00 [entrez]
AID - 10.1073/pnas.97.1.55 [doi]
PST - ppublish
SO  - Proc Natl Acad Sci U S A. 2000 Jan 4;97(1):55-60. doi: 10.1073/pnas.97.1.55.