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

. 2019 Sep 16;10:4216. doi: 10.1038/s41467-019-12110-y

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

© The Author(s) 2019

Open Access This article is licensed under a Creative Commons Attribution 4.0 International License, which permits use, sharing, adaptation, distribution and reproduction in any medium or format, as long as you give appropriate credit to the original author(s) and the source, provide a link to the Creative Commons license, and indicate if changes were made. The images or other third party material in this article are included in the article’s Creative Commons license, unless indicated otherwise in a credit line to the material. If material is not included in the article’s Creative Commons license and your intended use is not permitted by statutory regulation or exceeds the permitted use, you will need to obtain permission directly from the copyright holder. To view a copy of this license, visit http://creativecommons.org/licenses/by/4.0/.

PMC Copyright notice

Fig. 1 — SPA1 acts as a ser/thr protein kinase. a SPA1 kinase domain (SPA1-Kin) purified from E. coli showed an auto-phosphorylation activity in a concentration-dependent manner (autoradiogram on top panel). Bottom panel shows the protein level in a Coomassie-stained gel. M, indicates protein marker. b A conserved amino acid mutation on the SPA1 kinase domain reduces the auto-phosphorylation activity of SPA1 (autoradiogram on top panel). Bottom panel shows the protein level in a Coomassie-stained gel. c The N-terminal kinase domain of SPA1 exhibits kinase activity in the presence of myelin basic protein (MBP); a general kinase substrate (autoradiogram on top panel). Bottom panel shows the protein levels in a Coomassie-stained gel. d Full-length SPA1 purified from Pichia pastoris phosphorylates PIF1 in vitro (autoradiogram on top panel). Bottom panel shows the protein levels in a Coomassie-stained gel. e ATP-dependent kinase assays of full-length SPA1 on PIF1 (autoradiogram on top panel). ATP concentrations used were 0.004, 0.02, 0.1, 0.5, and 2.5 mM. Bottom panel shows the protein levels in a Coomassie-stained gel. f Kinetic analysis of the kinase activity of the full-length SPA1 on PIF1 (autoradiogram on top panel). Bottom panel shows the protein levels in a Coomassie-stained gel. g A conserved amino acid mutation on the full-length SPA1 kinase domain reduces the SPA1 kinase activity toward PIF1 (autoradiogram on top panel). Bottom panel shows the protein levels in a Coomassie-stained gel