دورية أكاديمية

Immunological detection of proteins similar to bacterial proteases in higher plant chloroplasts.

التفاصيل البيبلوغرافية
العنوان: Immunological detection of proteins similar to bacterial proteases in higher plant chloroplasts.
المؤلفون: OSTERSETZER, Oren, TABAK, Sarit, YARDEN, Oded, SHAPIRA, Roni, ADAM, Zach
المصدر: European Journal of Biochemistry; 3/15/96, Vol. 236 Issue 3, p932-936, 5p
مصطلحات موضوعية: PROTEOLYTIC enzymes, CHLOROPLASTS, ADENOSINE triphosphate, ESCHERICHIA coli, PLANTS, WESTERN immunoblotting, IMMUNOGLOBULINS, IMMUNOLOGY
مستخلص: Despite numerous demonstrations of protein degradation in chloroplasts of higher plants, little is known about the identity of the proteases involved in these reactions. To identify chloroplast proteases by immunological means, we investigated two proteins: ClpP, a protein similar to the proteolytic subunit of the bacterial ATP-dependent Clp protease, for which a gene is found in the chloroplast genome [Maurizi, M. R., Clark, W. P., Kim, S. H. & gottesman, S. (1990) J. Biol. Chem. 265,12546-12552] and prcA, a cyanobacterial Ca2+ -stimulated protease [Maldener, I., Lockau, W., Cai, Y. & Wolk, P. (1991) Mol. & Gen. Gener. 225, 113-120]. We expressed the clpP gene from rice in Escherichia coli, purified its product, and generated antibodies against the product. Western blot analysis revealed the ClpP protein in different leaf extracts. Analysis of fractionated barley chlorplasts revealed that the protein was associated with the stromal fraction. The expression of ClpP is light independent and tissue specific, and it was found in green and etiolated barley leaves, but not in roots. A second protein, similar to the cyanobacterial protease PrcA, was also detected in chloroplasts. Antibody against this protease recognized proteins in various leaf extracts. When pea chloroplast were fractionated, the antibody only recognized a stromal protein. The expression of the protein is regulated by light, as it was found in green leaves but not in etiolated leaves. The tissue specificity of PrcA was similar to that of ClpP in that it could not be detected in extracts. [ABSTRACT FROM AUTHOR]
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قاعدة البيانات: Complementary Index
الوصف
تدمد:00142956
DOI:10.1111/j.1432-1033.1996.00932.x