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TitleRedox Modulation of Oligomeric State in Proline Utilization A.
Journal, issue, pagesBiophys J, Vol. 114, Issue 12, Page 2833-2843, Year 2018
Publish dateJun 19, 2018
AuthorsDavid A Korasick / Ashley C Campbell / Shelbi L Christgen / Srinivas Chakravarthy / Tommi A White / Donald F Becker / John J Tanner /
PubMed AbstractHomooligomerization of proline utilization A (PutA) bifunctional flavoenzymes is intimately tied to catalytic function and substrate channeling. PutA from Bradyrhizobium japonicum (BjPutA) is unique ...Homooligomerization of proline utilization A (PutA) bifunctional flavoenzymes is intimately tied to catalytic function and substrate channeling. PutA from Bradyrhizobium japonicum (BjPutA) is unique among PutAs in that it forms a tetramer in solution. Curiously, a dimeric BjPutA hot spot mutant was previously shown to display wild-type catalytic activity despite lacking the tetrameric structure. These observations raised the question of what is the active oligomeric state of BjPutA. Herein, we investigate the factors that contribute to tetramerization of BjPutA in vitro. Negative-stain electron microscopy indicates that BjPutA is primarily dimeric at nanomolar concentrations, suggesting concentration-dependent tetramerization. Further, sedimentation-velocity analysis of BjPutA at high (micromolar) concentration reveals that although the binding of active-site ligands does not alter oligomeric state, reduction of the flavin adenine dinucleotide cofactor results in dimeric protein. Size-exclusion chromatography coupled with multiangle light scattering and small-angle x-ray scattering analysis also reveals that reduced BjPutA is dimeric. Taken together, these results suggest that the BjPutA oligomeric state is dependent upon both enzyme concentration and the redox state of the flavin cofactor. This is the first report, to our knowledge, of redox-linked oligomerization in the PutA family.
External linksBiophys J / PubMed:29925020 / PubMed Central
MethodsSAS (X-ray synchrotron)
Structure data

SASDDP3:
N-propargyl glycine-Inactivated Proline utilization A from Bradyrhizobium diazoefficiens (formerly Bradyrhizobium japonicum) collected by SEC-SAXS
Method: SAXS/SANS

SASDDQ3:
Proline utilization A from Bradyrhizobium diazoefficiens (formerly Bradyrhizobium japonicum) collected by SEC-SAXS
Method: SAXS/SANS

Source
  • Bradyrhizobium diazoefficiens (strain jcm 10833 / iam 13628 / nbrc 14792 / usda 110) (bacteria)

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