32kDa protein

In addition, the recent demonstration of the 32kDa protein as an essential component of the higher plant photosystem II reaction center (6,7) has added a new dimension to this interest with still broader implications for crop improvement in agriculture. 

Comparison of deduced amino acid sequences from psbA genes. Note the conservation of the PEST-1ike region contiguous with the a-helix-destabilizing, primary cleavage domain in the 32kDa protein. The arrow indicates the probable site where the precursor piece on the carboxy-terminus is cleaved (22). psbA sequences were compiled as follows (1) Anacystis nidulans copy I, and (2) copy II/III (41). 

Moreover, even in the precursor state, the stromal-lamellae associated protein shows similar trypsin-sensitive domains (P. Goloubinoff, unpublished). Hius, these data raise the possibility that membrane integration and orientation are independent of processing and translocation of the 32kDa protein. 

Cdc, cell division cycle DARPP-32, dopamine and cAMP-regulated phosphoprotein of 32kDa MAPK, mitogen-activated protein kinase NIPP1, nuclear inhibitor of PP1 PP, protein phosphatase Vffl, vaccinia virus. 

Hordenine Rt ° , Seedling Hordeum protein 26kDa Sd Hordeum protein 30kDa Sd Hordeum protein 32kDa Sd Hordeum thaumatin-like protein R Sd ° Hordeum thaumatin-like protein S Sd Hordeum vulgare protease inhibitor Fr °° Hordeum vulgare protein MW 28000 Sd w/o seedcoat ... 

Keyse SM, Tyrrell RM. Heme oxygenase is the major 32kDa stress protein induced in human skin fibroblasts by UVA radiation, hydrogen peroxide, and sodium arsenite. Proc. Natl. Acad. Sci. U.S.A. 1989 86 99-103. 

Precursor Processing. Hie precursor protein is synthesized on stromal lamellae and is processed there to the 32kDa mature form (21). Processing of the precursor is a posttranslational event (12) and takes place at the carboxy terminus (22). Following processing, the mature protein translocates to spatially-distinct chloroplast membranes, the grana, where functional photosystem II reaction centers are mainly located (21, 23). 

Comparison of aligned sequences in the PEST-1ike region of the 32kDa photosystem II reaction center protein with those of L subunit of Rhodopseudomonas capsulata (Lc). Adapted from ref. 38. 

Keyse SM, Tyrrell RM (1989) Heme oxygenase is the major 32Kda stress protein induced in human skin fibroblasts by UVA radiation, hydrogen peroxide and sodium arsenite. Proc Natl Acad Sci USA 86 99-103 Kier LE, Brusick DJ, Auletta AE, von Halle ES, Brown MM, Simmon VF, Dunkel V, McCann J, Mortelmans K, Prival M, Rao TK, Ray V (1986) The S. typhimuriumlmammalia microsomal assay. A report of the E.S. EPA Gene-Tox Program. Mutat Res 168 69-240... 

PSII (1). There are, however, other quinone-binding sites where the quinones are free to exchange with a mobile quinone population in the acyl lipid bilayer, e.g. the Qg site of the 32kDa herbicide-binding protein of PSll (1). 

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