Figure - PMC

Skip to main content

An official website of the United States government

Here's how you know

Here's how you know

Official websites use .gov
A .gov website belongs to an official government organization in the United States.

Secure .gov websites use HTTPS
A lock ( ) or https:// means you've safely connected to the .gov website. Share sensitive information only on official, secure websites.

View full-text article in PMC

. 2011 Sep 14;286(48):41368–41380. doi: 10.1074/jbc.M111.286690

Search in PMC
Search in PubMed
View in NLM Catalog
Add to search

© 2011 by The American Society for Biochemistry and Molecular Biology, Inc.

PMC Copyright notice

FIGURE 3. — The chain formation in STP mutants is attributed to CdhA controlled by SP-WalR. Shown is Western blotting of the extracellular fractions obtained from the wild-type M1SF370 and M1ΔSTP (A) and the wild-type M1T1 and M1T1ΔSTP (B) using anti-CdhA (SPy0019) antibody. The arrows indicate detection of an immunoreactive band at ∼45 kDa corresponding to CdhA. C, in vitro phosphorylation of SP-WalR by SP-STKK and dephosphorylation by SP-STP are shown in the autoradiogram. The arrows and arrowheads point toward the phosphorylated SP-STKK and SP-WalR, respectively. The parallel Coomassie-stained gel depicting the integrity of the proteins in each case is shown. M, migration of molecular mass standards. D, two-dimensional TLC of phosphorylated SP-WalR revealing phosphorylation at threonine in the autoradiogram and the migration of phosphoamino acid standards (tyrosine (pY), serine (pS), and threonine (pT)) by ninhydrin.