NDLI: Structure and function of the PsbP protein of Photosystem II from higher plants

Content Provider	Springer Nature Link
Author	Ifuku, Kentaro Nakatsu, Toru Shimamoto, Ren Yamamoto, Yumiko Ishihara, Seiko Kato, Hiroaki Sato, Fumihiko
Copyright Year	2005
Abstract	PsbP is a membrane extrinsic subunit of Photosystem II (PS II), which is involved in retaining Ca$^{2+}$ and Cl$^{−}$, two inorganic cofactors for the water-splitting reaction. In this study, we re-investigated the role of N-terminal region of PsbP on the basis of its three-dimensional structure. In previous paper [Ifuku and Sato (2002) Plant Cell Physiol 43: 1244–1249], a truncated PsbP lacking 19 N-terminal residues (Δ19) was found to bind to NaCl-washed PS II lacking PsbP and PsbQ without activation of oxygen evolution at all. Three-dimensional (3D) structure of PsbP suggests that deletion of 19 N-terminal residues would destabilize its protein structure, as indicated by the high sensitivity of Δ19 to trypsin digestion. Thus, a truncated PsbP lacking 15 N-terminal residues (Δ15), which retained core PsbP structure, was produced. Whereas Δ15 was resistant to trypsin digestion and bound to NaCl-washed PS II membranes, it did not show the activation of oxygen evolution. This result indicated that the interaction of 15-residue N-terminal flexible region of PsbP with PS II was important for Ca$^{2+}$ and Cl$^{−}$ retention in PS II, although the 15 N-terminal residues were not essential for the binding of PsbP to PS II. The possible N-terminal residues of PsbP that would be involved in this interaction are discussed.
Starting Page	251
Ending Page	255
Page Count	5
File Format	PDF
ISSN	01668595
Journal	Photosynthesis Research
Volume Number	84
Issue Number	1-3
e-ISSN	15735079
Language	English
Publisher	Kluwer Academic Publishers
Publisher Date	2005-01-01
Publisher Place	Dordrecht
Access Restriction	One Nation One Subscription (ONOS)
Subject Keyword	Calcium ion chloride ion crystal structure extrinsic protein higher plants Photosystem II PsbP Plant Physiology
Content Type	Text
Resource Type	Article
Subject	Cell Biology Plant Science Medicine Biochemistry

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