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PDBsum entry 1ej0
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Contents |
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* Residue conservation analysis
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References listed in PDB file
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Key reference
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Title
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Rna methylation under heat shock control.
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Authors
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H.Bügl,
E.B.Fauman,
B.L.Staker,
F.Zheng,
S.R.Kushner,
M.A.Saper,
J.C.Bardwell,
U.Jakob.
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Ref.
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Mol Cell, 2000,
6,
349-360.
[DOI no: ]
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PubMed id
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Abstract
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Structural, biochemical, and genetic techniques were applied to investigate the
function of FtsJ, a recently identified heat shock protein. FtsJ is well
conserved, from bacteria to humans. The 1.5 A crystal structure of FtsJ in
complex with its cofactor S-adenosylmethionine revealed that FtsJ has a
methyltransferase fold. The molecular surface of FtsJ exposes a putative nucleic
acid binding groove composed of highly conserved, positively charged residues.
Substrate analysis showed that FtsJ methylates 23S rRNA within 50S ribosomal
subunits in vitro and in vivo. Null mutations in ftsJ show a dramatically
altered ribosome profile, a severe growth disadvantage, and a
temperature-sensitive phenotype. Our results reveal an unexpected link between
the heat shock response and RNA metabolism.
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Figure 2.
Figure 2. FtsJ Has a Methyltransferase FoldStereo diagram
of the FtsJ tertiary fold highlighting secondary structure
elements. Secondary structures were assigned and the figure was
rendered by RIBBONS ([8]). The bound AdoMet is shown in ball and
stick representation.
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Figure 3.
Figure 3. AdoMet Binding Interactions in FtsJ(A) Stereo
diagram of the AdoMet binding site in FtsJ. In light blue are
the 2σ contours of F[o]–F[c] difference map (1.7 Å
native data) omitting AdoMet from the calculated structure
factors. AdoMet and FtsJ contact residues are shown in ball and
stick representation. Green, carbon (FtsJ); gray, carbon
(AdoMet); blue, nitrogen; yellow, sulfur; red, oxygen. Figure
drawn with RIBBONS.(B) Schematic diagram showing hydrogen bonds
and nonpolar contacts between FtsJ and the AdoMet cofactor
(green bonds). Black, carbon; blue, nitrogen; yellow, sulfur;
red, oxygen; purple, nonpolar contacts. Figure drawn with
LIGPLOT ([42]).
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The above figures are
reprinted
by permission from Cell Press:
Mol Cell
(2000,
6,
349-360)
copyright 2000.
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Secondary reference #1
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Title
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The ftsj/rrmj heat shock protein of escherichia coli is a 23 s ribosomal RNA methyltransferase.
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Authors
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T.Caldas,
E.Binet,
P.Bouloc,
A.Costa,
J.Desgres,
G.Richarme.
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Ref.
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J Biol Chem, 2000,
275,
16414-16419.
[DOI no: ]
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PubMed id
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Figure 5.
Fig. 5. Methylation of the 50 S ribosomal subunit by
RrmJ/FtsJ. 50 and 30 S ribosomal subunits from the
RrmJ-deficient strain were prepared and assayed for methylation
in the presence of RrmJ and [methyl-3H]AdoMet. Methylation of 50
S or 30 S ribosomal particles (0.8 pmol each) from the
RrmJ-deficient strain by purified RrmJ (2 pmol) was measured as
incorporation of 3H into a trichloroacetic acid precipitate in
10 min.
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Figure 7.
Fig. 7. Localization of the site of methylation by
RrmJ/FtsJ. 0.6 pmol of methyl-3H-labeled 23 S RNA, prepared
using RrmJ/FtsJ as described in legend to Fig. 6, was hybridized
with the indicated oligodeoxyribonucleotide and then digested
with RNase T1 (1-10 Sankyo units/pmol of RNA) as described under
"Experimental Procedures." Samples were precipitated with
trichloroacetic acid (TCA) and counted for radioactivity: no
oligomer (  circle ),
oligomer 1915 (  ),
oligomer 2449 (  ), and
oligomer 2552 (  ).
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The above figures are
reproduced from the cited reference
with permission from the ASBMB
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