Protein Information

Name protein is
Synonyms ANX 2; p36; LIP 2; LIP2; ANX2; ANX2L4; ANX2P1; ANX2P2…

Compound Information

Name diuron
CAS

Reference List

PubMed Abstract RScore(About this table)
7635157 Zer H, Ohad I: Photoinactivation of photosystem II induces changes in the photochemical reaction center II abolishing the regulatory role of the QB site in the D1 protein degradation. Eur J Biochem. 1995 Jul 15;231(2):448-53.

Tryptic digestion of the RCII-D1 protein is partially inhibited by diuron in isolated thylakoids [Trebst, A., Depka, B., Kraft, B. & Johanningmeier, U. (1988) Photosynth.
81(1,1,1,1) Details
3813542 Bhalla P, Bennett J: Chloroplast phosphoproteins: phosphorylation of a 12-kDa stromal protein by the redox-controlled kinase of thylakoid membranes. Arch Biochem Biophys. 1987 Jan;252(1):97-104.

When thylakoids and stroma are prepared from chloroplasts and are incubated with [gamma-32P] ATP in vitro, the 12-kDa protein is phosphorylated in the thylakoid preparation and then released from the membranes into the medium.
The electron transport inhibitor diuron blocks activation of the redox-controlled kinase and prevents phosphorylation of the 12-kDa protein, which is thus the first example of a soluble protein to be phosphorylated by the thylakoid-bound protein kinase.
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2121523 Teklemariam TA, Demeter S, Deak Z, Suranyi G, Borbely G: AS-1 cyanophage infection inhibits the photosynthetic electron flow of photosystem II in Synechococcus sp. FEBS Lett. 1990 Sep 17;270(1-2):211-5.


In addition, the breakdown of D1-protein is inhibited, comparable to DCMU-induced protection of D1-protein turnover, in AS-1-infected cells.
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12008895 Fulda S, Norling B, Schoor A, Hagemann M: The Slr0924 protein of Synechocystis sp. strain PCC 6803 resembles a subunit of the chloroplast protein import complex and is mainly localized in the thylakoid lumen. Plant Mol Biol. 2002 May;49(1):107-18.


Immunogold labelling of thin sections showed that the protein is located mainly in the thylakoid region.
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16453875 Brusslan J, Haselkorn R: Resistance to the photosystem II herbicide diuron is dominant to sensitivity in the cyanobacterium Synechococcus sp. EMBO J. 1989 Apr;8(4):1237-1245.

In Synechococcus 7942, the D1 protein is encoded by three functional genes called psbAI, psbAII and psbAIII.
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8425056 Bouyoub A, Vernotte C, Astier C: Functional analysis of the two homologous psbA gene copies in Synechocystis PCC 6714 and PCC 6803. Plant Mol Biol. 1993 Jan;21(2):249-58.


This protein is an essential subunit of photosystem II (PSII) and is the target for herbicides.
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8512617 Anbudurai PR, Pakrasi HB: Mutational analysis of the PsbL protein of photosystem II in the cyanobacterium Synechocystis sp. Z Naturforsch C. 1993 Mar-Apr;48(3-4):267-74.

Binding assays with radioactive diuron demonstrated that the mutant cells did not have any herbicide binding activity.
Our data indicate that the PsbL protein is essential for the normal functioning of PSII.
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18325336 Ferrario-Mery S, Meyer C, Hodges M: Chloroplast nitrite uptake is enhanced in Arabidopsis PII mutants. FEBS Lett. 2008 Apr 2;582(7):1061-6. Epub 2008 Mar 4.


In higher plants, the PII protein is a nuclear-encoded plastid protein that regulates the activity of a key enzyme of arginine biosynthesis.
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7853392 Kless H, Vermaas W: Many combinations of amino acid sequences in a conserved region of the D1 protein satisfy photosystem II function. J Mol Biol. 1995 Feb 10;246(1):120-31.


The putative de helix of the D1 protein is located at the acceptor side of photosystem II (PS II) and serves as an indispensable part of a niche that binds the secondary plastoquinone QB.
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7068652 Hoffman-Falk H, Mattoo AK, Marder JB, Edelman M, Ellis RJ: General occurrence and structural similarity of the rapidly synthesized, 32,000-dalton protein of the chloroplast membrane. J Biol Chem. 1982 Apr 25;257(8):4583-7.

Rapid synthesis of a 32,000-dalton plastid membrane protein is demonstrated for several diverse angiosperms and the alga, Chlamydomonas.
A rapidly metabolized membrane protein from Spirodela, with an apparent molecular weight of 32,000, has been implicated in allosterically regulating electron transport and mediating diuron herbicide sensitivity in the chloroplast (Mattoo, A.
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8068689 Kless H, Oren-Shamir M, Malkin S, McIntosh L, Edelman M: The D-E region of the D1 protein is involved in multiple quinone and herbicide interactions in photosystem II. Biochemistry. 1994 Aug 30;33(34):10501-7.

Mutation of codons Ser221 and Ser222 to Leu221 and Ala222 revealed a new location coordinating the herbicide diuron in the D1 protein.(ABSTRACT TRUNCATED AT 250 WORDS)
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7784425 Sobolev V, Edelman M: Modeling the quinone-B binding site of the photosystem-II reaction center using notions of complementarity and contact-surface between atoms. Proteins. 1995 Mar;21(3):214-25.


A model of the quinone (QB) binding site of the D1 protein is presented based upon the resolved structure of the QB binding pocket of the L subunit, and introducing novel quantitative notions of complementarity and contact surface between atoms.
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2842335 di Rago JP, Colson AM: Molecular basis for resistance to antimycin and diuron, Q-cycle inhibitors acting at the Qi site in the mitochondrial ubiquinol-cytochrome c reductase in Saccharomyces cerevisiae. J Biol Chem. 1988 Sep 5;263(25):12564-70.

Cytochrome b, a transmembranous protein, is thought to form a transmembrane electron circuit, transferring electrons between two ubiquinone redox sites, (Qi) and (Qo), respectively, near the inner and outer sides of the inner mitochondrial membrane.
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