Biochemical and Molecular Biological Study on Prenyltransferases of Entamoeba h stolytica
| Project/Area Number |
17590379
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| Research Category |
Grant-in-Aid for Scientific Research (C)
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| Allocation Type | Single-year Grants |
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| Section | 一般 |
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| Research Field |
Parasitology (including Sanitary zoology)
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| Research Institution | Jikei University School of Medicine |
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Principal Investigator |
KUMAGAI Masahiro Jikei University School of Medicine, School of Medicine, Assistant Professor (00271304)
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| Co-Investigator(Kenkyū-buntansha) |
MAKIKA Asao The Jikei University, School of Medicine, Associate Professor (90119850)
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| Project Period (FY) |
2005 – 2007
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| Project Status |
Completed (Fiscal Year 2007)
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| Budget Amount *help |
¥3,010,000 (Direct Cost: ¥2,800,000、Indirect Cost: ¥210,000)
Fiscal Year 2007: ¥910,000 (Direct Cost: ¥700,000、Indirect Cost: ¥210,000)
Fiscal Year 2006: ¥1,000,000 (Direct Cost: ¥1,000,000)
Fiscal Year 2005: ¥1,100,000 (Direct Cost: ¥1,100,000)
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| Keywords | Entamoeba histolytica / prenyltransferase / geranylgeranyltransferase / isoprenyl pyrophosphate synthetase / イソペンテニルニリン酸合成酵素 / ゲラニルゲラニルニリン酸合成酵素 / プレニル化酵素 / ゲラニルゲラニル化 |
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| Research Abstract |
We have been studying on the prenyltransferases from Entamoeba histolytica (Eh), and have previously reported that a protein farnesyltransferase from Eh does not farnesylate most of EhRas proteins, which have C-terminal amino acid of Leu or Phe. This is different from other organisms whose Ras proteins end with Ser and Met, and were farnesylated by a protein farnesyltransferase.
In this study, we revealed that Eh protein geranylgeranyltransferase type I geranylgeranylates EhRas proteins with Phe or Leu end That is, most Ras proteins are geranylgeranylated by a protein geranylgeranyltransferase type I in Eh. Then, we cloned and sequenced the Eh protein geranylgeranytransferase type II, and confirmed Rab escort protein dependent geranylgeranylation of Rab proteins by Eh protein geranylgeranyltransferase type II.
The homology search on the Eh database (x12 reads) revealed only 3 genes coding isoprenyl pyrophosphate synthetases (IPPS) with almost same amino acid sequences.
Farnesyl pyrophosphate synthetase (FPPS) and geranylgeranyl pyrophosphate synthetase (GGPPS) from various organisms separated into 3 major clades in a phylogenetic tree. Those clade were FPPS ; GGPPS from mammals, fishes, and yeasts ; and GGPP from bacteria. The IPPS from Eh and its relative species Entamoeba disparbranched out long from a side of the clades of bacterial GGPPS, suggesting that IPPS from Eh is GGPPS which locates in a phiylogenetically distinctive position.
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Report
(4 results)
Research Products
(49 results)
