scholarly journals Genomic organization, sequence analysis and expression of all five genes encoding the small subunit of ribulose-1,5-bisphosphate carboxylase/oxygenase from tomato

1987 ◽  
Vol 209 (2) ◽  
pp. 247-256 ◽  
Author(s):  
Mamoru Sugita ◽  
Thianda Manzara ◽  
Eran Pichersky ◽  
Anthony Cashmore ◽  
Wilhelm Gruissem
1986 ◽  
Vol 6 (7) ◽  
pp. 2347-2353
Author(s):  
J O Berry ◽  
B J Nikolau ◽  
J P Carr ◽  
D F Klessig

The regulation of the genes encoding the large and small subunits of ribulose 1,5-bisphosphate carboxylase was examined in amaranth cotyledons in response to changes in illumination. When dark-grown cotyledons were transferred into light, synthesis of the large- and small-subunit polypeptides was initiated very rapidly, before any increase in the levels of their corresponding mRNAs. Similarly, when light-grown cotyledons were transferred to total darkness, synthesis of the large- and small-subunit proteins was rapidly depressed without changes in mRNA levels for either subunit. In vitro translation or in vivo pulse-chase experiments indicated that these apparent changes in protein synthesis were not due to alterations in the functionality of the mRNAs or to protein turnover, respectively. These results, in combination with our previous studies, suggest that the expression of ribulose 1,5-bisphosphate carboxylase genes can be adjusted rapidly at the translational level and over a longer period through changes in mRNA accumulation.


1986 ◽  
Vol 6 (7) ◽  
pp. 2347-2353 ◽  
Author(s):  
J O Berry ◽  
B J Nikolau ◽  
J P Carr ◽  
D F Klessig

The regulation of the genes encoding the large and small subunits of ribulose 1,5-bisphosphate carboxylase was examined in amaranth cotyledons in response to changes in illumination. When dark-grown cotyledons were transferred into light, synthesis of the large- and small-subunit polypeptides was initiated very rapidly, before any increase in the levels of their corresponding mRNAs. Similarly, when light-grown cotyledons were transferred to total darkness, synthesis of the large- and small-subunit proteins was rapidly depressed without changes in mRNA levels for either subunit. In vitro translation or in vivo pulse-chase experiments indicated that these apparent changes in protein synthesis were not due to alterations in the functionality of the mRNAs or to protein turnover, respectively. These results, in combination with our previous studies, suggest that the expression of ribulose 1,5-bisphosphate carboxylase genes can be adjusted rapidly at the translational level and over a longer period through changes in mRNA accumulation.


Gene ◽  
1986 ◽  
Vol 48 (1) ◽  
pp. 23-32 ◽  
Author(s):  
Thomas D. McKnight ◽  
Danny C. Alexander ◽  
Marla S. Babcock ◽  
Robert B. Simpson

1990 ◽  
Vol 15 (1) ◽  
pp. 49-58 ◽  
Author(s):  
Jane Silverthorne ◽  
Charles F. Wimpee ◽  
Takashi Yamada ◽  
Stephen A. Rolfe ◽  
Elaine M. Tobin

2005 ◽  
Vol 187 (11) ◽  
pp. 3884-3888 ◽  
Author(s):  
Svetlana N. Dedysh ◽  
Ksenia V. Smirnova ◽  
Valentina N. Khmelenina ◽  
Natalia E. Suzina ◽  
Werner Liesack ◽  
...  

ABSTRACT Representatives of the genus Beijerinckia are known as heterotrophic, dinitrogen-fixing bacteria which utilize a wide range of multicarbon compounds. Here we show that at least one of the currently known species of this genus, i.e., Beijerinckia mobilis, is also capable of methylotrophic metabolism coupled with the ribulose bisphosphate (RuBP) pathway of C1 assimilation. A complete suite of dehydrogenases commonly involved in the sequential oxidation of methanol via formaldehyde and formate to CO2 was detected in cell extracts of B. mobilis grown on CH3OH. Carbon dioxide produced by oxidation of methanol was further assimilated via the RuBP pathway as evidenced by reasonably high activities of phosphoribulokinase and ribulose-1,5-bisphosphate carboxylase/oxygenase (RubisCO). Detection and partial sequence analysis of genes encoding the large subunits of methanol dehydrogenase (mxaF) and form I RubisCO (cbbL) provided genotypic evidence for methylotrophic autotrophy in B. mobilis.


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