| Item type |
デフォルトアイテムタイプ_（フル）(1) |
| 公開日 |
2023-03-18 |
| タイトル |
|
|
タイトル |
New aspects of sterol carrier protein 2 (nonspecific lipid-transfer protein) in fusion proteins and in peroxisomes |
|
言語 |
en |
| 作成者 |
Bun-ya, Masanori
Muro, Yoshitaka
Niki, Toshiro
Kondo, Jun
Kamiryo, Tatsuyuki
|
| アクセス権 |
|
|
アクセス権 |
open access |
|
アクセス権URI |
http://purl.org/coar/access_right/c_abf2 |
| 権利情報 |
|
|
権利情報 |
Copyright (c) 2000 Humana Press |
| 主題 |
|
|
主題Scheme |
Other |
|
主題 |
sterol carrier protein 2 |
| 主題 |
|
|
主題Scheme |
Other |
|
主題 |
SCP2 |
| 主題 |
|
|
主題Scheme |
Other |
|
主題 |
thiolase |
| 主題 |
|
|
主題Scheme |
Other |
|
主題 |
molecular chaperone |
| 主題 |
|
|
主題Scheme |
Other |
|
主題 |
bile acid |
| 主題 |
|
|
主題Scheme |
NDC |
|
主題 |
460 |
| 内容記述 |
|
|
内容記述 |
Sterol carrier protein 2 (SCP2) is a 13-kDa peroxisomal protein, identical to nonspecific lipid-transfer protein, and stimulates various steps of cholesterol metabolism in vitro. Although the name is reminiscent of acyl carrier protein, which is involved in fatty acid synthesis, SCP2 does not bind to lipids specifically or stoichiometrically. This protein is expressed either as a small precursor or as a large fusion (termed SCPx) that carries at its C-terminal the complete sequence of SCP2. SCPx exhibits 3-oxoacyl-CoA thiolase activity, as well as sterol-carrier and lipid-transfer activities. The N- and C-terminal parts of SCPx are similar to the nematode protein P-44 and the yeast protein PXP-18, respectively. P-44, which has no SCP2 sequence, thiolytically cleaved the side chain of bile acid intermediate at a rate comparable to that of SCPx. This, together with the properties of other fusions with SCP2-like sequence, suggests that the SCP2 part of SCPx does not play a direct role in thiolase reaction. PXP-18, located predominantly inside peroxisomes, is similar to SCP2 in primary structure and lipid-transfer activity, and protects peroxisomal acyl-CoA oxidase from thermal denaturation. PXP-18 dimerized at a high temperature, formed an equimolar complex with the oxidase subunit, and released the active enzyme from the complex when the temperature went down. This article attempts to gain insight into the role of SCP2, and to present a model in which PXP-18, a member of the SCP2 family, functions as a molecular chaperone in peroxisomes. |
|
言語 |
en |
| 出版者 |
|
|
出版者 |
Humana Press |
| 言語 |
|
|
言語 |
eng |
| 資源タイプ |
|
|
資源タイプ識別子 |
http://purl.org/coar/resource_type/c_6501 |
|
資源タイプ |
journal article |
| 出版タイプ |
|
|
出版タイプ |
AO |
|
出版タイプResource |
http://purl.org/coar/version/c_b1a7d7d4d402bcce |
| 関連情報 |
|
|
|
識別子タイプ |
PMID |
|
|
関連識別子 |
11330036 |
| 関連情報 |
|
|
|
識別子タイプ |
DOI |
|
|
関連識別子 |
10.1385/CBB:32:1-3:107 |
| 関連情報 |
|
|
関連タイプ |
isVersionOf |
|
|
識別子タイプ |
DOI |
|
|
関連識別子 |
http://dx.doi.org/10.1385/CBB:32:1-3:107 |
| 収録物識別子 |
|
|
収録物識別子タイプ |
NCID |
|
収録物識別子 |
AA11112602 |
| 収録物識別子 |
|
|
収録物識別子タイプ |
ISSN |
|
収録物識別子 |
1085-9195 |
| 開始ページ |
|
|
開始ページ |
107 |
| 書誌情報 |
Cell Biochemistry and Biophysics
Cell Biochemistry and Biophysics
巻 32,
p. 107-116,
発行日 2000
|
| 旧ID |
24945 |
CBB_32_107.pdf (870.9 KB)
