Functional analysis of the Rubisco large subunit  N-methyltransferase promoter from tobacco and its regulation by light in soybean hairy roots

1998 ◽  
Vol 17 (12) ◽  
pp. 907-912 ◽  
Author(s):  
M. Mazarei ◽  
Z. Ying ◽  
R. L. Houtz
Keyword(s):  
Functional Analysis ◽  
Hairy Roots ◽  
Large Subunit ◽  
Subunit A

Structural Properties and Ribulosebisphosphate Carboxylase and Oxygenase Activity of Fraction-1 Protein from the Marine Alga Halimeda cylindracea (Chlorophyta)

1976 ◽  
Vol 3 (1) ◽  
pp. 93 ◽  
Author(s):  
T Akazawa ◽  
CB Osmond
Keyword(s):  
Large Subunit ◽  
Homogeneous State ◽  
Plant Type ◽  
Precipitation Line ◽  
Carboxylase Activity ◽  
Bisphosphate Carboxylase ◽  
Subunit A ◽  
Fraction 1 Protein ◽  
Oxygenase Activity ◽  
Ribulosebisphosphate Carboxylase

Ribulosebisphosphate carboxylase/oxygenase activity was detected in Halimeda cylindracea and Chaetomorpha crassa. In H. cylindracea carboxylase activity (72-250 micromoles CO2 fixed per hour per milligram chlorophyll) was sufficient to account for measured photosynthetic rates. The activity of the oxygenase was only 1 % that of the carboxylase but otherwise both enzymes showed properties similar to those of the same enzymes in higher green plants. Fraction-1 protein from H. cylindracea was purified to a homogeneous state as tested by poly- acrylamide gel electrophoresis at pH 8.9. The activity of the ribulose-1,5-bisphosphate carboxylase in the purified preparations was 0.1 micromoles CO2 fixed per minute per milligram protein (pH 7.0). The H. cylindracea fraction-1 protein was shown to comprise two subunits, A and B, with molecular weights 5.4 × 104, and 1.35 x 104, respectively, typical of the plant-type ribulose-1,5-bisphosphate carboxylase. The amino acid composition of the large subunit A was similar to that from spinach and Chlorella enzymes, whereas that of the subunit B was markedly distinguishable from the enzymes of other origins. The close resemblance of the H. cylindricea protein to the plant enzymes was further supported by the formation of a spur in the double immunodiffusion precipitation line, indicating probable existence of sequence-homology of the catalytic larger subunit A, typical of the plant-type enzyme molecules.

scholarly journals Functional Analysis of the Terminase Large Subunit, G2P, ofBacillus subtilisBacteriophage SPP1

2000 ◽  
Vol 275 (45) ◽  
pp. 35311-35319 ◽  
Author(s):  
Aranzazu Gual ◽  
Ana G. Camacho ◽  
Juan C. Alonso
Keyword(s):  
Functional Analysis ◽  
Large Subunit

Human Gene for the Large Subunit of Ribonucleotide Reductase (RRM1): Functional Analysis of the Promoter

Genomics ◽  
1995 ◽  
Vol 27 (2) ◽  
pp. 280-285 ◽  
Author(s):  
Nigel J. Parker ◽  
C.Glenn Begley ◽  
Richard M. Fox
Keyword(s):  
Functional Analysis ◽  
Ribonucleotide Reductase ◽  
Human Gene ◽  
Large Subunit

Agrobacterium rhizogenes-mediated transformation of Prunus as an alternative for gene functional analysis in hairy-roots and composite plants

2011 ◽  
Vol 30 (7) ◽  
pp. 1313-1326 ◽  
Author(s):  
Nathalie Bosselut ◽  
Cyril Van Ghelder ◽  
Michel Claverie ◽  
Roger Voisin ◽  
Jean-Paul Onesto ◽  
...  
Keyword(s):  
Functional Analysis ◽  
Agrobacterium Rhizogenes ◽  
Hairy Roots ◽  
Composite Plants ◽  
Gene Functional Analysis

Hairy Roots as a Tool for the Functional Analysis of Plant Genes

Hairy Roots ◽  
2018 ◽  
pp. 275-292 ◽  
Author(s):  
Chonglu Zhong ◽  
Mathish Nambiar-Veetil ◽  
Didier Bogusz ◽  
Claudine Franche
Keyword(s):  
Functional Analysis ◽  
Hairy Roots ◽  
Plant Genes

The Ancient Heart of the Ribosomal Large Subunit: A Response to Caetano-Anolles

2015 ◽  
Vol 80 (3-4) ◽  
pp. 166-170 ◽  
Author(s):  
Anton S. Petrov ◽  
Loren Dean Williams
Keyword(s):  
Large Subunit ◽  
Subunit A

Depletion and Reconstitution of Active E. Coli Ribosomes

1975 ◽  
Vol 33 ◽  
pp. 640-641
Author(s):  
M. Boublik ◽  
W. Hellmann ◽  
F. Jenkins
Keyword(s):  
Protein Biosynthesis ◽  
Large Subunit ◽  
High Resolution Electron Microscopy ◽  
Small Subunit ◽  
Structure And Function ◽  
Biologically Active ◽  
Biological Macromolecules ◽  
E Coli ◽  
Resolution Electron ◽  
And Function

Correlations between structure and function of biological macromolecules have been studied intensively for many years, mostly by indirect methods. High resolution electron microscopy is a unique tool which can provide such information directly by comparing the conformation of biopolymers in their biologically active and inactive state. We have correlated the structure and function of ribosomes, ribonucleoprotein particles which are the site of protein biosynthesis. 70S E. coli ribosomes, used in this experiment, are composed of two subunits - large (50S) and small (30S). The large subunit consists of 34 proteins and two different ribonucleic acid molecules. The small subunit contains 21 proteins and one RNA molecule. All proteins (with the exception of L7 and L12) are present in one copy per ribosome.This study deals with the changes in the fine structure of E. coli ribosomes depleted of proteins L7 and L12. These proteins are unique in many aspects.

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