PMID- 10459008
OWN - NLM
STAT- MEDLINE
DCOM- 19990923
LR  - 20190508
IS  - 0021-9525 (Print)
IS  - 0021-9525 (Linking)
VI  - 146
IP  - 4
DP  - 1999 Aug 23
TI  - The ribosome regulates the GTPase of the beta-subunit of the signal recognition
      particle receptor.
PG  - 723-30
AB  - Protein targeting to the membrane of the ER is regulated by three GTPases, the
      54-kD subunit of the signal recognition particle (SRP) and the alpha- and
      beta-subunit of the SRP receptor (SR). Here, we report on the GTPase cycle of the
      beta-subunits of the SR (SRbeta). We found that SRbeta binds GTP with high
      affinity and interacts with ribosomes in the GTP-bound state. Subsequently, the
      ribosome increases the GTPase activity of SRbeta and thus functions as a GTPase
      activating protein for SRbeta. Furthermore, the interaction between SRbeta and
      the ribosome leads to a reduction in the affinity of SRbeta for guanine
      nucleotides. We propose that SRbeta regulates the interaction of SR with the
      ribosome and thereby allows SRalpha to scan membrane-bound ribosomes for the
      presence of SRP. Interaction between SRP and SRalpha then leads to release of the
      signal sequence from SRP and insertion into the translocon. GTP hydrolysis then
      results in dissociation of SR from the ribosome, and SRP from the SR.
FAU - Bacher, G
AU  - Bacher G
AD  - Zentrum fur Molekulare Biologie der Universitat Heidelberg, D-69052 Heidelberg,
      Germany.
FAU - Pool, M
AU  - Pool M
FAU - Dobberstein, B
AU  - Dobberstein B
LA  - eng
PT  - Journal Article
PT  - Research Support, Non-U.S. Gov't
PL  - United States
TA  - J Cell Biol
JT  - The Journal of cell biology
JID - 0375356
RN  - 0 (GTPase-Activating Proteins)
RN  - 0 (Liposomes)
RN  - 0 (Membrane Glycoproteins)
RN  - 0 (Membrane Proteins)
RN  - 0 (Molecular Chaperones)
RN  - 0 (Proteins)
RN  - 0 (Receptors, Cytoplasmic and Nuclear)
RN  - 0 (Receptors, Peptide)
RN  - 0 (SEC Translocation Channels)
RN  - 0 (Trans-Activators)
RN  - 0 (nascent-polypeptide-associated complex)
RN  - 0 (signal peptide receptor)
RN  - 146-91-8 (Guanosine Diphosphate)
RN  - 147096-90-0 (TRAM protein, ER, mammalian)
RN  - 34273-04-6 (Guanylyl Imidodiphosphate)
RN  - 86-01-1 (Guanosine Triphosphate)
RN  - EC 3.6.1.- (GTP Phosphohydrolases)
SB  - IM
MH  - Animals
MH  - Binding Sites
MH  - Dogs
MH  - Endoplasmic Reticulum, Rough/metabolism
MH  - GTP Phosphohydrolases/*metabolism
MH  - GTPase-Activating Proteins
MH  - Guanosine Diphosphate/metabolism
MH  - Guanosine Triphosphate/*metabolism
MH  - Guanylyl Imidodiphosphate/metabolism
MH  - Hydrolysis
MH  - Liposomes/metabolism
MH  - Membrane Glycoproteins/metabolism
MH  - Membrane Proteins/metabolism
MH  - Microsomes
MH  - Models, Biological
MH  - Molecular Chaperones
MH  - Protein Binding
MH  - Proteins/metabolism
MH  - Receptors, Cytoplasmic and Nuclear/genetics/*metabolism
MH  - Receptors, Peptide/genetics/*metabolism
MH  - Ribosomes/*metabolism
MH  - SEC Translocation Channels
MH  - Sequence Deletion
MH  - Trans-Activators/metabolism
PMC - PMC2156146
EDAT- 1999/08/25 00:00
MHDA- 1999/08/25 00:01
CRDT- 1999/08/25 00:00
PHST- 1999/08/25 00:00 [pubmed]
PHST- 1999/08/25 00:01 [medline]
PHST- 1999/08/25 00:00 [entrez]
AID - 10.1083/jcb.146.4.723 [doi]
PST - ppublish
SO  - J Cell Biol. 1999 Aug 23;146(4):723-30. doi: 10.1083/jcb.146.4.723.