Journal article
The propensity of the bacterial rodlin protein RdlB to form amyloid fibrils determines its function in Streptomyces coelicolor
W Yang, J Willemse, EB Sawyer, F Lou, W Gong, H Zhang, SL Gras, D Claessen, S Perrett
Scientific Reports | NATURE PORTFOLIO | Published : 2017
DOI: 10.1038/srep42867
Abstract
Streptomyces bacteria form reproductive aerial hyphae that are covered with a pattern of pairwise aligned fibrils called rodlets. The presence of the rodlet layer requires two homologous rodlin proteins, RdlA and RdlB, and the functional amyloid chaplin proteins, ChpA-H. In contrast to the redundancy shared among the eight chaplins, both RdlA and RdlB are indispensable for the establishment of this rodlet structure. By using a comprehensive biophysical approach combined with in vivo characterization we found that RdlB, but not RdlA, readily assembles into amyloid fibrils. The marked difference in amyloid propensity between these highly similar proteins could be largely attributed to a differ..
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Awarded by Australian Research Council
Funding Acknowledgements
The X-ray diffraction data was collected on the macromolecular crystallography beamline (MX2) at the Australian Synchrotron, Victoria, Australia. The authors wish to acknowledge the MX2 beamline staff for their support. This work was supported by a Major International Collaborative Grant from the National Natural Science Foundation of China [31110103914] and by the Chinese Ministry of Science 973 Program [2013CB910700, 2012CB911000] to S.P.; and by the Netherlands Organization for Scientific Research (NWO) via a VIDI grant (12957) to D.C. SG is supported by The ARC Dairy Innovation Hub (IH120100005).