PMID- 8263910
OWN - NLM
STAT- MEDLINE
DCOM- 19940124
LR  - 20191210
IS  - 0022-2836 (Print)
IS  - 0022-2836 (Linking)
VI  - 234
IP  - 4
DP  - 1993 Dec 20
TI  - Ribosomal proteins L11 and L10.(L12)4 and the antibiotic thiostrepton interact 
      with overlapping regions of the 23 S rRNA backbone in the ribosomal GTPase 
      centre.
PG  - 1013-20
AB  - The Escherichia coli ribosomal protein (r-protein) L11 and its binding site on 23 
      S ribosomal RNA (rRNA) are associated with ribosomal hydrolysis of guanosine 
      5'-triphosphate (GTP). We have used hydroxyl radical footprinting to map the 
      contacts between L11 and the backbone riboses in 23 S rRNA, and to investigate 
      how this interaction is influenced by other ribosomal components. Complexes were 
      characterized in both naked 23 S rRNA and ribosomes from an E. coli L11-minus 
      strain, before and after reconstitution with L11. The protein protects 17 riboses 
      between positions 1058 and 1085 in the naked 23 S rRNA. Within the ribosome, L11 
      also interacts with this rRNA region, although the protection effects are subtly 
      different and extend to nucleotide 1098. The pentameric r-protein complex 
      L10.(L12)4 binds to an adjacent site on the rRNA, protecting riboses at positions 
      1043, 1046 to 1049, 1053 to 1055 and increasing the accessibility of position 
      1068. The overlap in the positions affected by r-proteins L11 and L10.(L12)4, and 
      the increase in protection between positions 1078 and 1084 when they are bound at 
      the same time, reflect the mutually cooperative nature of their interaction with 
      the rRNA. The data support a model for the tertiary configuration of the rRNA 
      region, in which two stem-loop structures fold so that the loops lie in close 
      proximity, with the main ribose interactions of L11 within the minor groove of 
      one of the stems. The conformation of the rRNA-L11 interaction is modulated by 
      L10.(L12)4 and other proteins within the ribosome. The antibiotics thiostrepton 
      and micrococcin inhibit the catalytic functions of this region by slotting in 
      between the accessible loops and interacting with nucleotides there.
FAU - Rosendahl, G
AU  - Rosendahl G
AD  - Department of Molecular Biology, Odense University, Denmark.
FAU - Douthwaite, S
AU  - Douthwaite S
LA  - eng
PT  - Journal Article
PT  - Research Support, Non-U.S. Gov't
PL  - Netherlands
TA  - J Mol Biol
JT  - Journal of molecular biology
JID - 2985088R
RN  - 0 (Fungal Proteins)
RN  - 0 (RNA, Ribosomal, 23S)
RN  - 0 (Ribosomal Proteins)
RN  - 0 (ribosomal protein L11)
RN  - 1407-48-3 (alpha-sarcin)
RN  - 70815-33-7 (ribosomal protein L7-L12)
RN  - EC 3.1.- (Endoribonucleases)
RN  - EC 3.6.1.- (GTP Phosphohydrolases)
RN  - HR4S203Y18 (Thiostrepton)
SB  - IM
MH  - Base Sequence
MH  - Binding Sites
MH  - *Endoribonucleases
MH  - Escherichia coli
MH  - Fungal Proteins/metabolism
MH  - GTP Phosphohydrolases/chemistry
MH  - Molecular Sequence Data
MH  - Nucleic Acid Conformation
MH  - Protein Binding
MH  - RNA, Ribosomal, 23S/*metabolism/ultrastructure
MH  - Ribosomal Protein L10
MH  - Ribosomal Proteins/*metabolism
MH  - Ribosomes/drug effects/metabolism/*ultrastructure
MH  - Thiostrepton/*metabolism
EDAT- 1993/12/20 00:00
MHDA- 1993/12/20 00:01
CRDT- 1993/12/20 00:00
PHST- 1993/12/20 00:00 [pubmed]
PHST- 1993/12/20 00:01 [medline]
PHST- 1993/12/20 00:00 [entrez]
AID - S0022-2836(83)71655-4 [pii]
AID - 10.1006/jmbi.1993.1655 [doi]
PST - ppublish
SO  - J Mol Biol. 1993 Dec 20;234(4):1013-20. doi: 10.1006/jmbi.1993.1655.