Degradation of D2 protein due to UV-B irradiation of the reaction centre of photosystem II

G. Friso; R. Barbato; G. M. Giacometti; J. Barber

doi:10.1016/0014-5793(94)80419-2

Degradation of D2 protein due to UV-B irradiation of the reaction centre of photosystem II

G. Friso, R. Barbato, G. M. Giacometti, J. Barber

Risultato della ricerca: Contributo su rivista › Articolo in rivista › peer review

Abstract

Exposure of isolated reaction centres of photosystem II to UV-B radiation generates specific breakdown products of the D2 protein. When the quinone, 2,5-dibromo-3-methyl-6-isopropyl-p-benzoquinone is present a 22 kDa fragment containing the N-terminus of the mature protein is generated. Concomitant with the appearance of the N-terminal fragment, two fragments containing the C-terminus of the D2 protein having apparent molecular masses around 10-12 kDa are observed. It is concluded that the primary cleavage occurs in the hydrophilic loop linking putative transmembrane segments IV and V. No such cleavage was observed when silicomolybdate was used as an electron acceptor, suggesting that this UV-B damage is dependent on binding of the added quinone to the Q_A site.

Lingua originale	Inglese
pagine (da-a)	217-221
Numero di pagine	5
Rivista	FEBS Letters
Volume	339
Numero di pubblicazione	3
DOI	https://doi.org/10.1016/0014-5793(94)80419-2
Stato di pubblicazione	Pubblicato - 21 feb 1994
Pubblicato esternamente	Sì

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10.1016/0014-5793(94)80419-2

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title = "Degradation of D2 protein due to UV-B irradiation of the reaction centre of photosystem II",

abstract = "Exposure of isolated reaction centres of photosystem II to UV-B radiation generates specific breakdown products of the D2 protein. When the quinone, 2,5-dibromo-3-methyl-6-isopropyl-p-benzoquinone is present a 22 kDa fragment containing the N-terminus of the mature protein is generated. Concomitant with the appearance of the N-terminal fragment, two fragments containing the C-terminus of the D2 protein having apparent molecular masses around 10-12 kDa are observed. It is concluded that the primary cleavage occurs in the hydrophilic loop linking putative transmembrane segments IV and V. No such cleavage was observed when silicomolybdate was used as an electron acceptor, suggesting that this UV-B damage is dependent on binding of the added quinone to the QA site.",

keywords = "D2 protein, Photoinactivation, Photosystem II, UVB light",

author = "G. Friso and R. Barbato and Giacometti, {G. M.} and J. Barber",

note = "Funding Information: Acknowledgements. The present work has partially been supported by the PNRA (National Program for Antartic Research). We also wish to thank the Agricultural and Food Research Council (J.B.). During this work R.B. was the recipient of a short term fellowship from the European Molecular Biology Organisation: G.F. was the recipient of a fellowship from the Federation of European Biochemical Societies. which allowed much of the work to be conducted at Imperial College.",

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doi = "10.1016/0014-5793(94)80419-2",

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T1 - Degradation of D2 protein due to UV-B irradiation of the reaction centre of photosystem II

AU - Friso, G.

AU - Barbato, R.

AU - Giacometti, G. M.

AU - Barber, J.

N1 - Funding Information: Acknowledgements. The present work has partially been supported by the PNRA (National Program for Antartic Research). We also wish to thank the Agricultural and Food Research Council (J.B.). During this work R.B. was the recipient of a short term fellowship from the European Molecular Biology Organisation: G.F. was the recipient of a fellowship from the Federation of European Biochemical Societies. which allowed much of the work to be conducted at Imperial College.

PY - 1994/2/21

Y1 - 1994/2/21

N2 - Exposure of isolated reaction centres of photosystem II to UV-B radiation generates specific breakdown products of the D2 protein. When the quinone, 2,5-dibromo-3-methyl-6-isopropyl-p-benzoquinone is present a 22 kDa fragment containing the N-terminus of the mature protein is generated. Concomitant with the appearance of the N-terminal fragment, two fragments containing the C-terminus of the D2 protein having apparent molecular masses around 10-12 kDa are observed. It is concluded that the primary cleavage occurs in the hydrophilic loop linking putative transmembrane segments IV and V. No such cleavage was observed when silicomolybdate was used as an electron acceptor, suggesting that this UV-B damage is dependent on binding of the added quinone to the QA site.

AB - Exposure of isolated reaction centres of photosystem II to UV-B radiation generates specific breakdown products of the D2 protein. When the quinone, 2,5-dibromo-3-methyl-6-isopropyl-p-benzoquinone is present a 22 kDa fragment containing the N-terminus of the mature protein is generated. Concomitant with the appearance of the N-terminal fragment, two fragments containing the C-terminus of the D2 protein having apparent molecular masses around 10-12 kDa are observed. It is concluded that the primary cleavage occurs in the hydrophilic loop linking putative transmembrane segments IV and V. No such cleavage was observed when silicomolybdate was used as an electron acceptor, suggesting that this UV-B damage is dependent on binding of the added quinone to the QA site.

KW - D2 protein

KW - Photoinactivation

KW - Photosystem II

KW - UVB light

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U2 - 10.1016/0014-5793(94)80419-2

DO - 10.1016/0014-5793(94)80419-2

M3 - Article

SN - 0014-5793

VL - 339

SP - 217

EP - 221

JO - FEBS Letters

JF - FEBS Letters

IS - 3

ER -

Degradation of D2 protein due to UV-B irradiation of the reaction centre of photosystem II

Abstract

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