They are interested. in the structure of the ACDS (Acetyl-CoA Decarbonylase SYnd'ase) multienzyme complex which is responsible for the synthesis and cleavage of acetyl-CoA in methanogens. To determine the detailed oligorneric structure of the complex ( -1.6-2 MDA), accurate molecular masses are needed. ACDS complexes from Methanosarcina therinophila and M. barkeri contain five different subunits designated -a, P, y, 6, and F- The complex can also be dissociated into three protein subcomponents, one of which is (a + e). It is thought that the (a+e) particle is a heterotetramer (oc2e2) of approximately 220 kDa, but gel filtration data have indicated a value of 350 kDa. To start this project, fi-eeze-dried specimens of the (a+c:) particle were prepared. Preliminary ma s measurements indicate that it is a heterotetramer. The (y + 8) subcomponent from the complex has also been examined in the STEM for mass analysis, which is being performed now.

Agency
National Institute of Health (NIH)
Institute
National Center for Research Resources (NCRR)
Type
Biotechnology Resource Grants (P41)
Project #
5P41RR001777-18
Application #
6308944
Study Section
Project Start
2000-04-01
Project End
2001-03-31
Budget Start
1998-10-01
Budget End
1999-09-30
Support Year
18
Fiscal Year
2000
Total Cost
$9,722
Indirect Cost
Name
Brookhaven National Laboratory
Department
Type
DUNS #
027579460
City
Upton
State
NY
Country
United States
Zip Code
11973
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