They are interested in the structure of the ACDS (Acetyl-CoA Decarbonylase Synthase) multienzyme complex which is responsible for the synthesis and cleavage of acetyl-CoA in methanogens. To determine the detailed oligomeric structure of the complex (~1 .6-2 M[)a), accurate molecular masses are needed. ACDS complexes from Methanosarcina therniophila and M bUNIT contain five different subunits designated ~, ~, y, 6, and E. The complex can also be dissociated into three protein subcomponents, one of which is (~ + e). It is thought that the (~+E) particle is a heterotetramer (~2E2) of approximately 220 k')a, but gel filtration data have indicated a value of 350 k')a. To start this project, freeze-dried specimens of the (~+E) particle were prepared. Preliminary mass measurements indicate that it is a heterotetramer.

Agency
National Institute of Health (NIH)
Institute
National Center for Research Resources (NCRR)
Type
Biotechnology Resource Grants (P41)
Project #
2P41RR001777-15
Application #
2805052
Study Section
Project Start
Project End
Budget Start
1996-10-01
Budget End
1997-09-30
Support Year
15
Fiscal Year
1997
Total Cost
Indirect Cost
Name
Brookhaven National Laboratory
Department
Type
DUNS #
027579460
City
Upton
State
NY
Country
United States
Zip Code
11973
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