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. Author manuscript; available in PMC: 2021 May 9.
Published in final edited form as: Nat Microbiol. 2020 Nov 9;6(1):34–43. doi: 10.1038/s41564-020-00808-5

Extended Data Fig. 5. Nascent peptidoglycan is the preferred substrate of SagB-SpdC.

Extended Data Fig. 5

Cold glycan strands were prepared with radiolabeled wall teichoic acid (lanes 2–5) and incubated with a hydrolase. In the presence of either SagB (lane 3) or SagB-SpdC (lane 4), the ladder signal remained the same as a no treatment control (lane 2). There was reduced radiolabeled signal towards the top of the gel in both reactions; this signal represents a population of longer peptidoglycan oligomers and the fainter signal suggests less wall teichoic acid present. In contrast, mutanolysin was able to hydrolyze wall teichoic acid-modified glycan strands. To test whether SagB-SpdC cleavage interfered with wall teichoic acid ligation, cold oligomers were prepared and then incubated with radiolabeled wall teichoic precursor, LIIAWTA, and the wall teichoic acid ligase, TagT. The appearance of the radiolabeled ladder indicates that SagB-SpdC products were ligated with wall teichoic acid (lane 9).