2004 Fiscal Year Final Research Report Summary
Establishment of methods for prediction of the function of functionally-unknown gene products by the analysis of the posttranslational protein modifications.
Project/Area Number |
15580080
|
Research Category |
Grant-in-Aid for Scientific Research (C)
|
Allocation Type | Single-year Grants |
Section | 一般 |
Research Field |
Applied biochemistry
|
Research Institution | Yamaguchi University |
Principal Investigator |
UTSUMI Toshihiko Yamaguchi University, Department of Biological Chemistry, Faculty of Agriculture, Professor, 農学部, 教授 (20168727)
|
Project Period (FY) |
2003 – 2004
|
Keywords | prediction / protein function / functionally-unknown protein / posttranslational modification / protein N-myristoylation / modification signal |
Research Abstract |
Upon the completion of the Human Genome Project, huge numbers of genetic sequences are now available. However, the function of many of these genes has not been identified. Therefore, the identification of the function of these genes is one of the most important purposes of the study of Proteomics. Now, it is well known that many of the posttranslational modifications such as proteolytic processing, phosphorylation, glycosylation, lipid modifications, ADP-ribosylation etc. play critical roles in the structure and function of protein and regulate many cellular events such as intracellular signal transduction. However, systematic method to analyze the posttranslational modification of protein has not been established. In the present study, we have shown that targeting, processing and modification of a distinct protein could be successfully detected by using metabolic labeling in an in vitro translation system or in transfected cells. Since many of these posttranslational modifications play specific roles in the structure and function of protein, it might be possible to predict the function of the protein from these experimental observations.
|
Research Products
(15 results)
-
-
[Journal Article] N-terminus of B96Bom, a Bombyx mori G-protein-coupled receptor, is N-myristoylated and translocated across the membrane.2005
Author(s)
Utsumi, T., Ohta, H., Kayano, Y., Sakural, N., Ozoe, Y.
-
Journal Title
FEBS Journal 272
Pages: 472-481
Description
「研究成果報告書概要(欧文)」より
-
-
-
[Journal Article] Oxidative stress underlies the mechanism for Ca^<2+>- induced permeability transition of mitochondria.2004
Author(s)
Kanno, T., Sato, E.F., Muranaka, S., Fujita, H., Utsumi, T., Inoue, M., Utsumi, K.
-
Journal Title
Free Rad.Res. 38
Pages: 27-35
Description
「研究成果報告書概要(欧文)」より
-
[Journal Article] Vertical-scanning mutagenesis of amino acids in a model N-myristoylation motif reveals the major amino-terminal sequence requirements for protein N-myristoylation.2004
Author(s)
Utsumi, T., Nakano, K., Funakoshi, T., Kayano, Y., Nakao, S., Sakurai, N., Iwata, H., Ishisaka, R.
-
Journal Title
Eur.J.Biochem. 271
Pages: 863-874
Description
「研究成果報告書概要(欧文)」より
-
-
-
-
-
-
[Journal Article] Mechanism of enhanced apoptosis in HL-60 cells by UV-irradiated n-3 and n-6 polyunsaturated fatty acids.2003
Author(s)
Arita, K., Yamamoto, Y., Takehara, Y., Utsumi, T., Kanno, T., Miyaguchi, C., Akiyama, J., Yoshioka, T., Utsumi, K.
-
Journal Title
Free Radic.Biol.Med. 35
Pages: 189-199
Description
「研究成果報告書概要(欧文)」より
-
[Journal Article] Topogenesis of two transmembrane type K^+ channels, Kir2.1 and KcsA.2003
Author(s)
Umigai, N., Sato, Y., Mizutani, A., Utsumi, T., Sakaguchi, M., Uozumi, N.
-
Journal Title
J.Biol.Chem. 278
Pages: 40373-40384
Description
「研究成果報告書概要(欧文)」より
-
[Journal Article] Involvement of Ras/Extracellular signal-regulated kinase, but not Akt pathway in risedronate-induced apoptosis of U937 cells and its suppression by cytochalasin B.
Author(s)
Fujita, H., Utsumi, T., Muranaka, S., Ogino, T., Yano, H., Akiyama, J., Yasuda, T., Utsumi, K.
-
Journal Title
Biochem Pharmacol. (In press)
Description
「研究成果報告書概要(欧文)」より
-