Novel isoprenoid modified proteins in Halobacteria.
Incorporation of [3H]mevalonic acid-derived materials into proteins was studied with extremely halophilic archaebacteria, Halobacterium halobium and Halobacterium cutirubrum. Several labeled proteins were detected on SDS-polyacrylamide gel electrophoresis followed by fluorography. The majority of the radioactive materials released from the labeled proteins by sulfonium salt cleavage moved with a mobility similar to that of a C85 polyprenol on reverse-phase thin-layer chromatography, and no radioactive farnesol was found on the chromatography. However, a weak but significant protein farnesyltransferase activity was detected in in vitro experiments with a combination of [3H]farnesyl diphosphate and Ras precursor protein.
Sagami
H
H
Institute for Chemical Reaction Science, Tohoku University, Sendai, Japan.
Kikuchi
A
A
Ogura
K
K
Fushihara
K
K
Nishino
T
T
D019883:Alkyl and Aryl Transferases; D001426:Bacterial Proteins / Q000378:metabolism*; D004591:Electrophoresis, Polyacrylamide Gel; D051231:Farnesyltranstransferase; D006217:Halobacterium / Q000201:enzymology / Q000378:metabolism*; D019617:Halobacterium salinarum / Q000201:enzymology / Q000378:metabolism; D008798:Mevalonic Acid / Q000378:metabolism; D011106:Polyisoprenyl Phosphates / Q000378:metabolism; D017368:Protein Prenylation; D012717:Sesquiterpenes; D014166:Transferases / Q000378:metabolism
D001426:Bacterial Proteins; D011106:Polyisoprenyl Phosphates; D012717:Sesquiterpenes; C004808:farnesyl pyrophosphate; D014166:Transferases; D019883:Alkyl and Aryl Transferases; D051231:Farnesyltranstransferase; D008798:Mevalonic Acid