JOURNAL ARTICLE

Molecular Bulkiness of a Single Amino Acid in the F1 α-Subunit Determines the Robustness of Cyanobacterial ATP Synthase.

  • Published In: Plant & Cell Physiology, 2023, v. 64, n. 12. P. 1590 1 of 3

  • Database: Academic Search Ultimate 2 of 3

  • Authored By: Machida, Akito; Kondo, Kumiko; Wakabayashi, Ken-ichi; Tanaka, Kan; Hisabori, Toru 3 of 3

Abstract

This article investigates the role of an amino acid substitution at position 252 in the α-subunit of cyanobacterial FoF1 ATP synthase (CyFoF1), focusing on its impact on growth, enzyme complex levels, and activity in Synechocystis sp. PCC 6803 (S. 6803). The substitution of tyrosine (Tyr) with cysteine (Cys) at this position (αY252C), previously identified in Synechococcus elongatus PCC 7942 (S. 7942), was introduced into S. 6803 to assess its generality across cyanobacteria. Results showed that αY252C decreased growth rate and high-light tolerance and significantly reduced the membrane-bound CyFoF1 complex level without affecting ATP synthase enzymatic activity or intracellular ATP levels. Structural predictions indicated no major conformational changes in the α-subunit, suggesting that the substitution impairs enzyme complex formation or stability rather than catalytic function, highlighting the importance of the amino acid side chain bulkiness at position 252 for cyanobacterial growth and ATP synthase assembly.

Additional Information

  • Source:Plant & Cell Physiology. 2023/12, Vol. 64, Issue 12, p1590
  • Document Type:Article
  • Subject Area:Chemistry
  • Publication Date:2023
  • ISSN:0032-0781
  • DOI:10.1093/pcp/pcad109
  • Accession Number:174386742
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