Effects of a-amanitin on coordination of two mRNAs of ribulose-bisphosphate carboxylase in greening pea leaves

نویسنده

  • Yukiko Sasaki
چکیده

The effects of cr-amanitin on light induction of the two mRNAs of ribulose-bisphosphate carboxylase/oxygenase (RuBisCO) in greening pea leaves were examined. Induction of the nuclear-coded small-subunit mRNA but not of the chloroplast-coded large-subunit mRNA was significantly reduced by a-amanitin, indicating that the steady-state level of the large-subunit mRNA is not directly affected by that of the small subunit. This suggests that there is no direct link between nuclear transcription and light induction of the large-subunit mRNA. The synthesis of RuBisCO was also slowed in proportion to the small-subunit mRNA level, and there was not a large excess of the unassociated large subunit polypeptide. The synthesis of the two subunits is probably coordinated. Thus, the expression of the large subunit is partly controlled at the post-transcriptional level.

برای دانلود متن کامل این مقاله و بیش از 32 میلیون مقاله دیگر ابتدا ثبت نام کنید

ثبت نام

اگر عضو سایت هستید لطفا وارد حساب کاربری خود شوید

منابع مشابه

SYNTHESIS OF THE SMALL SUBUNIT OF RIBULOSE 1, 5-DIPHOSPHATE CARBOXYLASE ON CYTOPLASMIC RIBOSOMES FROM G R E E N I N G BEAN LEAVES J.C. GRAY* and R.G.O. KEKWICK

Ribulose I, 5-diphosphate carboxylase (EC 4.1.1.39) is the most abundant protein in the leaves of higher plants, where it is confined to the chloroplasts. The enzyme is composed of two types of subunits which differ in size [1, 2]. The differential labelling of amino acids in the two subunits on incorporation of 14CO2 by'tobacco leaves suggested the possibility that the two subunits were synthe...

متن کامل

Isolation and some properties of ribulose-1, 5-bisphosphate carboxylase-oxygenase from red kidney bean primary leaves.

Purification of ribulose-1,5-bisphosphate carboxylase from primary leaves of Phaseolus vulgaris var. Red Kidney with ammonium sulfate precipitation, ion exchange chromatography, and gel filtration resulted in the complete loss of detectable oxygenase activity and the retention of a low velocity and a high K(m) form of both the carboxylase and oxygenase. The polyethylene glycol-6000-purified rib...

متن کامل

Electron microscopy of the complexes of ribulose-1,5-bisphosphate carboxylase (Rubisco) and Rubisco subunit-binding protein from pea leaves.

The structure of ribulose-1,5-bisphosphate carboxylase (Rubisco) subunit-binding protein and its interaction with pea leaf chloroplast Rubisco were studied by electron microscopy and image analysis. Electron-microscopic evidence for the association of Rubisco subunit-binding protein, consisting of 14 subunits arranged with 72 point group symmetry, and oligomeric (L8S8) Rubisco was obtained.

متن کامل

Correlation of Carbonic Anhydrase and Ribulose-1,5-Bisphosphate Carboxylase/Oxygenase Expression in Pea.

The enzyme carbonic anhydrase (carbonate dehydratase, EC 4.2.1.1) is an abundant soluble protein in the C3 plant chloroplast; however, its function in photosynthetic carbon assimilation is not well defined. In this study we have examined the relationship between carbonic anhydrase (CA) and ribulose-1,5-bisphosphate carboxylase/oxygenase (Rubisco) expression during pea (Pisum sativum) developmen...

متن کامل

The Formation of Ribulose Diphosphate Carboxylase Protein during Chloroplast Development in Barley.

Ribulose 1,5-diphosphate carboxylase is synthesized in barley leaves growing in the dark. Upon illumination there is a marked increase in the rate of synthesis of the enzyme. The specific activity of the enzyme expressed as cpm incorporated into phosphoglyceric acid per mug of fraction I protein, after isolation shows no change either during dark growth or greening. During early stages of illum...

متن کامل

ذخیره در منابع من


  با ذخیره ی این منبع در منابع من، دسترسی به آن را برای استفاده های بعدی آسان تر کنید

برای دانلود متن کامل این مقاله و بیش از 32 میلیون مقاله دیگر ابتدا ثبت نام کنید

ثبت نام

اگر عضو سایت هستید لطفا وارد حساب کاربری خود شوید

عنوان ژورنال:

دوره   شماره 

صفحات  -

تاریخ انتشار 2001