Abstract
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.
Publication types
-
Research Support, Non-U.S. Gov't
-
Research Support, U.S. Gov't, P.H.S.
MeSH terms
-
Amino Acid Sequence
-
Animals
-
Arabidopsis / genetics
-
Bacterial Proteins / chemistry*
-
Bacterial Proteins / metabolism*
-
Caenorhabditis elegans / genetics
-
Crystallography, X-Ray
-
Escherichia coli / genetics
-
Heat-Shock Proteins / chemistry*
-
Heat-Shock Proteins / metabolism*
-
Humans
-
Methanococcus / genetics
-
Methylation
-
Methyltransferases / chemistry
-
Methyltransferases / metabolism*
-
Models, Molecular
-
Molecular Sequence Data
-
Open Reading Frames
-
Protein Structure, Secondary
-
RNA, Ribosomal, 23S / metabolism
-
Recombinant Proteins / chemistry
-
Recombinant Proteins / metabolism
-
Ribosomes / metabolism
-
S-Adenosylmethionine / metabolism
-
Schizosaccharomyces / genetics
-
Sequence Alignment
-
Sequence Homology, Amino Acid
Substances
-
Bacterial Proteins
-
Heat-Shock Proteins
-
RNA, Ribosomal, 23S
-
Recombinant Proteins
-
S-Adenosylmethionine
-
Methyltransferases