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2 in 1: One-step Affinity Purification for the Parallel Analysis of Protein-Protein and Protein-Metabolite Complexes
Published on: August 6, 2018
Processing of PatS, a morphogen precursor, in cell extracts of Anabaena sp. PCC 7120
Lianglin Zhang1, Fang Zhou1, Shuai Wang1
1State Key Laboratory of Freshwater Ecology and Biotechnology, Institute of Hydrobiology, Chinese Academy of Sciences, Wuhan, China.
Abstract:
Upon N-stepdown, Anabaena sp. PCC 7120 differentiates heterocysts along filaments in a semiregular pattern. A 17-amino acid peptide called PatS is a morphogen precursor for pattern formation. The principal PatS derivative involved in heterocyst patterning has been proposed to be the C-terminal peptide PatS-5 (RGSGR), PatS-6 (ERGSGR), or PatS-8 (CDERGSGR). We present the first evidence for processing of PatS in cell extracts of this cyanobacterium. PatS is probably cleaved between the C-terminal 7th and 8th amino acid residues, producing PatS-7 (DERGSGR), then converted into PatS-6 and PatS-5. The processing site could be changed by a substitution at the C-terminal 8th residue.

