Novel isoprenoid modified proteins in halobacteria

Hiroshi Sagami; Akihiro Kikuchi; Kyozo Ogura; Kazuhisa Fushihara; Tokuzo Nishino

doi:10.1006/bbrc.1994.2277

Novel isoprenoid modified proteins in halobacteria

Hiroshi Sagami, Akihiro Kikuchi, Kyozo Ogura, Kazuhisa Fushihara, Tokuzo Nishino

Institute of Multidisciplinary Research for Advanced Materials (IMRAM)

Research output: Contribution to journal › Article › peer-review

6 Citations (Scopus)

Abstract

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.

Original language	English
Pages (from-to)	972-978
Number of pages	7
Journal	Biochemical and biophysical research communications
Volume	203
Issue number	2
DOIs	https://doi.org/10.1006/bbrc.1994.2277
Publication status	Published - 1994 Sep 15

ASJC Scopus subject areas

Biophysics
Biochemistry
Molecular Biology
Cell Biology

Access to Document

10.1006/bbrc.1994.2277

Fingerprint Dive into the research topics of 'Novel isoprenoid modified proteins in halobacteria'. Together they form a unique fingerprint.

Cite this

@article{da59348e73e14facaa559ded33ffc9bc,

title = "Novel isoprenoid modified proteins in halobacteria",

abstract = "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.",

author = "Hiroshi Sagami and Akihiro Kikuchi and Kyozo Ogura and Kazuhisa Fushihara and Tokuzo Nishino",

year = "1994",

month = sep,

day = "15",

doi = "10.1006/bbrc.1994.2277",

language = "English",

volume = "203",

pages = "972--978",

journal = "Biochemical and Biophysical Research Communications",

issn = "0006-291X",

publisher = "Academic Press Inc.",

number = "2",

}

TY - JOUR

T1 - Novel isoprenoid modified proteins in halobacteria

AU - Sagami, Hiroshi

AU - Kikuchi, Akihiro

AU - Ogura, Kyozo

AU - Fushihara, Kazuhisa

AU - Nishino, Tokuzo

PY - 1994/9/15

Y1 - 1994/9/15

N2 - 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.

AB - 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.

UR - http://www.scopus.com/inward/record.url?scp=0027990380&partnerID=8YFLogxK

UR - http://www.scopus.com/inward/citedby.url?scp=0027990380&partnerID=8YFLogxK

U2 - 10.1006/bbrc.1994.2277

DO - 10.1006/bbrc.1994.2277

M3 - Article

C2 - 8093082

AN - SCOPUS:0027990380

VL - 203

SP - 972

EP - 978

JO - Biochemical and Biophysical Research Communications

JF - Biochemical and Biophysical Research Communications

SN - 0006-291X

IS - 2

ER -