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

. 2023 Nov 28;223(2):e202211026. doi: 10.1083/jcb.202211026

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

© 2023 Mahone et al.

This article is distributed under the terms of an Attribution–Noncommercial–Share Alike–No Mirror Sites license for the first six months after the publication date (see http://www.rupress.org/terms/). After six months it is available under a Creative Commons License (Attribution–Noncommercial–Share Alike 4.0 International license, as described at https://creativecommons.org/licenses/by-nc-sa/4.0/).

PMC Copyright notice

Figure 7. — FzlA interacts with FtsK_C via the FzlA C-terminal tail. (A and B) Western blots of whole cell lysates or eluates from an immunoprecipitation (IP) using α-FLAG resin. Ladder values to the left of the blots are in kDa. Red arrows to the right of the blots indicate to what protein the band is attributed. The presence or absence of the fusion proteins in the strains used are indicated above the blots by plus (+) or minus (−) signs, respectively. (A) 3xFLAG-FzlA immunoprecipitation. Blots were incubated with primary antibodies recognizing either mCherry (αRFP) or FLAG (αFLAG). Lane 1 and 4, fzlA::3xFLAG-fzlA (EG2217). Lane 2 and 5, ftsK:: ftsK-mChy (EG2427). Lane 3 and 6, fzlA::3xFLAG-fzlA; ftsK:: ftsK-mChy (EG2428). (B) FtsK-FLAG immunoprecipitation. Blots were incubated with primary antibodies recognizing either FzlA (αFzlA) or FLAG (αFLAG). Lane 1 and 3, WT (EG865). Lane 2 and 4, ftsK::ftsK-FLAG (EG742). (C) BTH results for interaction between FzlA variants and full-length FtsK or its domains. The adenylyl cyclase subunits T18 (left) and T25 (top) are fused to proteins via the N-terminus or C-terminus, respectively. A green box around the representative spot image indicates that the three biological triplicates were positive for induction of the cAMP-dependent β-galactosidase reporter, indicating a positive interaction. Some data in C is duplicated in Fig. S5 A. Source data are available for this figure: SourceData F7.