Modulation of oat mitochondrial ATPase activity by CA2+ and phytochrome.

Serlin, Bruce S.; Sopory, Sudhir K.; Roux, Stanley J.

doi:10.1104/pp.74.4.827

Cited by 28 publications

(11 citation statements)

References 28 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…These differences in the kinetics between the alpha and the beta subunits may be attributable to the fact that the alpha subunit is mitochondrial-encoded [5] and the beta subunit nuclear-encoded [3]. It is interesting to note that our data on the effects of light on ATPase message levels parallel observations by Serlin et al [15] who report that red light, via phytochrome, depressed ATPase activity in isolated mitochondria.…”

Section: Discussionsupporting

confidence: 78%

Light-regulated protein and mRNA synthesis in root caps of maize

1988

View full text Add to dashboard Cite

Illumination of maize roots initiates changes in mRNA levels and in the activities of proteins within the root cap. Using Northern analysis we showed a 5-6 fold increase in the levels of three specific mRNAs and a 14-fold increase in plastid mRNA. This increase is rapid, occurring within 30 minutes of illumination. With prolonged periods of darkness following illumination, messages return to levels observed in dark, control caps. For two species of mRNA illumination results in a reduction in message levels. Light-stimulated increases in the levels of specific mRNAs are proportionally greater than are increases in the activities of corresponding proteins. We suggest that the light-stimulated increase in protein activity in root caps may be preceded by and occur as a consequence of enhanced levels of mRNA. Our work suggests that photomorphogenesis in roots could involve changes in the levels of a wide variety of mRNAs within the root cap.

show abstract

Section: Discussionsupporting

confidence: 78%

Light-regulated protein and mRNA synthesis in root caps of maize

1988

View full text Add to dashboard Cite

show abstract

“…By elimination, it appears that some of the calmodulin is located between the inner and outer membranes. Such calmodulin could be linked to phytochromecontrolled calcium movements into and out ofthe mitochondria (21) and calcium-modulated ATPase activity (24).…”

Section: Resultsmentioning

confidence: 99%

“…Etioplasts were isolated by the method of Jacobson (I 1), using 8-d-old etiolated leaf tissue. Mitochondria were isolated from chilled 4-d-old etiolated oat tissue as described previously (24). Outer mitochondrial membranes and mitoplasts were prepared by the methods of Moreau and Lance (17).…”

mentioning

confidence: 99%

Characterization of Oat Calmodulin and Radioimmunoassay of Its Subcellular Distribution

Biro

Daye²,

Serlin³

et al. 1984

Plant Physiol.

101

View full text Add to dashboard Cite

A protein identifiable as calmodulin has been isolated from oat (Avena sativa, var Garry) tissues. This protein is relatively heat stable, binds to hydrophobic gels, and phenothiazines in a calcium-dependent fashion, and binds to antibody to rat testes calmodulin. Based on its migration on sodium dodecyl sulfate-polyacrylamide gels, ultraviolet absorption spectrum, and amino acid composition, oat calmodulin is essentially identical to calmodulin isolated from other higher plants. Radioimmunoassays indicate that calmodulin is associated with isolated oat protoplasts, mitochondria, etioplasts, and nuclei and also appears to be a component of oat cell wall fractions.Much evidence has accumulated recently to support the hypothesis that Ca 2 plays a major role in mediating the adaptations of plants to certain environmental changes (12,22). As in animals, at least some Ca2-imediated responses in plants are controlled by Ca2-binding regulatory proteins. Among these, the most studied and best characterized is calmodulin (1).We have published reports suggesting a possible role for calmodulin in mediating phytochrome and gravitropic responses in Avena saliva (oats) (2, 21). As part of our ongoing research on this question, we have isolated and characterized calmodulin from oats and have estimated its content, both in intact tissue and in isolated subcellular fractions, by radioimmunoassay. Here we report the results of these experiments.MATERIALS AND METHODS Plant Material. Except where indicated, the starting material for all extractions was taken from the coleoptiles and primary leaves of 3-to 4-d-old dark-grown oat (A vena sativa, var. Garry) seedlings, harvested 5 to 7.5 mm above the seed. The oats were grown on water-saturated vermiculite at 27C.Calmodulin Isolation. Two extraction methods were employed.'Supported by grants from the National Aeronautics and Space Administration (NSG 7480), The National Science Foundation (PCM 81-03429), and The Robert A. Welch Foundation (F 858) to S. J. R.

show abstract

“…1988). Regulations of protein phosphorylation have also been reported to be associated with phytochrome-modulated red/far-red light irradiation in etiolated coleoptile, mitochondria and nuclei of oat seedlings (Serlin et al, 1984;Datta et af., 1985;Schaefer, 1987), and maize protoplasts (Das and Sopory, 1985). In addition, Wong et al (1986) reported that a polycation-dependent protein kinase is present in highly purified preparations of phytochrome.…”

Section: Introductionmentioning

confidence: 99%

A PURIFIED 124‐kDa OAT PHYTOCHROME DOES NOT POSSESS A PROTEIN KINASE ACTIVITY*

Kim¹,

Bai²,

Song³

1989

Photochem & Photobiology

View full text Add to dashboard Cite

The presence of protein kinase activity in the purified phytochrome preparations [Wong, et al. (1986) J. Biol. Chem. 261, 12089-12097] has been re-examined. The phytochrome preparations having SAR (specific absorbance ratio, A668/A280 for the Pr form as a measure of phytochrome purity) values of greater than 0.95 were homogeneous on SDS gel, but could be further purified to a SAR value of 1.07 by repeated gel filtrations on a Bio-Gel A-0.5 m column. The protein kinase activity remained in the phytochrome preparations having SAR values less than 1.05, but it became undetectable in the phytochrome preparation with a SAR value of 1.07. Two dimensional gel electrophoresis of the phytochrome preparation (SAR, 0.89) showed that a phytochrome band with pl 5.8 had no kinase activity. Phosphorylating activity of the protein kinase was enhanced to some extent by polycations, polylysine and histone. Phytochrome served as a good substrate for this enzyme. The present data indicate that phytochrome has no intrinsic protein kinase activity, but a protein kinase is present in highly purified phytochrome preparations.

show abstract

Modulation of oat mitochondrial ATPase activity by CA2+ and phytochrome.

Cited by 28 publications

References 28 publications

Light-regulated protein and mRNA synthesis in root caps of maize

Light-regulated protein and mRNA synthesis in root caps of maize

Characterization of Oat Calmodulin and Radioimmunoassay of Its Subcellular Distribution

A PURIFIED 124‐kDa OAT PHYTOCHROME DOES NOT POSSESS A PROTEIN KINASE ACTIVITY*

Contact Info

Product

Resources

About