1998 Fiscal Year Final Research Report Summary
Studies on A-factor receptor protein involved in secondary metabolism and morphorogical differentiation in Streptomyces griseus
| Project/Area Number |
09306005
|
|---|
| Research Category |
Grant-in-Aid for Scientific Research (A)
|
| Allocation Type | Single-year Grants |
|---|
| Section | 一般 |
|---|
| Research Field |
応用微生物学・応用生物化学
|
|---|
| Research Institution | The University of Tokyo |
|---|
Principal Investigator |
HORINOUCHI Sueharu The University of Tokyo, Graduate School of Agriculture and Life Sciences.Professor, 大学院・農学生命科学研究科, 教授 (80143410)
|
|---|
| Project Period (FY) |
1997 – 1998
|
| Keywords | Streptomyces griseus / A-factor / Receptor Protein / Secondary Metabolism / Morphorogical Differentiation / X-ray crystallography |
|---|
| Research Abstract |
A-factor is a representative of the autoregulatory factors, often called microbial hormones, that switch on secondary metabolism and morphogenesis in the bacterial genus Streptomyces. In Streptomyces griseus, A-factor at an extremely low concentration triggers streptomycin (Sm) production and cell differentiation by binding a repressor-type receptor protein (ArpA) and dissociating it from DNA.The purpose of this study is revealing the molecular function of ArpA.
1. The target genes of ArpA
An A-factor-responsive transcriptional activator (AdpA) able to bind the promoter of strR, a pathway-specific regulatory gene responsible for transcription of other Sm biosynthetic genes, was found to be the target of ArpA.This result can explain how A-factor triggers Sm biosynthesis at a late exponential growth stage.
Two DNA fragments which contain ArpA-binding site were cloned from the genome of S.griseus. Transcriptional analysis of some candidates of ArpA-target gene are proceeding. Gene disruption of these genes are also proceeding.
2.3D-structure of a microbial hormone receptor
Crystallization of an ArpA homologue (CrpB) of Streptomyces coelicolor was successfully achieved. Crystallographic parameters and initial phases were determined using X-ray diffraction. In near future, 3D-structure of CrpB will be revealed. Then 3D-structure of ArpA may be solved easily.
|
