Abstract:
:Assembly of protein complexes is a key mechanism for achieving spatial and temporal coordination in processes involving many enzymes. Growth of rod-shaped bacteria is a well-studied example requiring such coordination; expansion of the cell wall is thought to involve coordination of the activity of synthetic enzymes with the cytoskeleton via a stable complex. Here, we use single-molecule tracking to demonstrate that the bacterial actin homolog MreB and the essential cell wall enzyme PBP2 move on timescales orders of magnitude apart, with drastically different characteristic motions. Our observations suggest that PBP2 interacts with the rest of the synthesis machinery through a dynamic cycle of transient association. Consistent with this model, growth is robust to large fluctuations in PBP2 abundance. In contrast to stable complex formation, dynamic association of PBP2 is less dependent on the function of other components of the synthesis machinery, and buffers spatially distributed growth against fluctuations in pathway component concentrations and the presence of defective components. Dynamic association could generally represent an efficient strategy for spatiotemporal coordination of protein activities, especially when excess concentrations of system components are inhibitory to the overall process or deleterious to the cell.
journal_name
Proc Natl Acad Sci U S Aauthors
Lee TK,Tropini C,Hsin J,Desmarais SM,Ursell TS,Gong E,Gitai Z,Monds RD,Huang KCdoi
10.1073/pnas.1313826111subject
Has Abstractpub_date
2014-03-25 00:00:00pages
4554-9issue
12eissn
0027-8424issn
1091-6490pii
1313826111journal_volume
111pub_type
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