Co-Expression of a Precursor and the Mature Protein of Wheat Ribulose-1, 5-bisphosphate Carboxylase Small Subunit from a Single Gene inEscherichia coli

1990 ◽  
Vol 9 (1) ◽  
pp. 11-25 ◽  
Author(s):  
MUSTAK A. KADERBHAI ◽  
MINGYUE HE ◽  
R. BRIAN BEECHEY ◽  
NAHEED KADERBHAI
Keyword(s):  
Single Gene ◽  
Small Subunit ◽  
Inescherichia Coli ◽  
Mature Protein ◽  
Bisphosphate Carboxylase ◽  
Ribulose 1

Dual targeting ability of targeting signals is dependent on the nature of the mature protein

2003 ◽  
Vol 30 (7) ◽  
pp. 805 ◽  
Author(s):  
Orinda Chew ◽  
James Whelan
Keyword(s):  
Alternative Oxidase ◽  
Small Subunit ◽  
Trna Synthetase ◽  
Mature Protein ◽  
Bisphosphate Carboxylase ◽  
Dual Targeting ◽  
Targeting Signal ◽  
Targeting Signals ◽  
Targeting Ability ◽  
Passenger Protein

The targeting ability of three signals previously shown to support the import of passenger proteins into both mitochondria and chloroplasts was investigated with authentic mitochondrial or chloroplastic proteins. An in vitro dual import assay that maintained import specificity showed that the ability of dual signals to support mitochondrial and chloroplastic import depended on the nature of the passenger protein. All dual targeting signals supported import of their native mature protein as a passenger into both mitochondria and chloroplasts. However the glutathione reductase targeting signal only supported mitochondrial import with the mitochondrial protein alternative oxidase, and chloroplast import with the small subunit of ribulose-1,5-bisphosphate carboxylase / oxygenase. The Arabidopsis histidyl-tRNA synthetase targeting signal only supported mitochondrial import with the alternative oxidase as a passenger, but the small subunit of ribulose-1,5-bisphosphate carboxylase / oxygenase was imported into both mitochondria and chloroplasts. The Arabidopsis asparaginyl-tRNA synthetase supported import of alternative oxidase and the small subunit of ribulose-1,5-bisphosphate carboxylase / oxygenase into both mitochondria and chloroplasts. Analysis of the targeting signals of all known dual targeted proteins using targeting predictions indicates that most of them are more strongly predicted to be chloroplast-targeted. Secondary structure predictions indicate the ability of most dual targeted signals to form both α-helical and β-sheet-type structures, a feature of mitochondrial and plastid targeting signals, respectively. Thus, it appears that a major determinant of dual targeting ability is the nature of the mature or passenger protein.

scholarly journals Targeted knockdown of ribulose-1, 5-bisphosphate carboxylase-oxygenase in rice mesophyll cells impact on photosynthesis and growth

2020 ◽  
Author(s):  
Chirag Maheshwari ◽  
Robert A Coe ◽  
Shanta Karki ◽  
Sarah Covshoff ◽  
Ronald Tapia ◽  
...  
Keyword(s):  
Protein Content ◽  
Biomass Accumulation ◽  
Transcript Abundance ◽  
Small Subunit ◽  
Assimilation Rate ◽  
Mesophyll Cells ◽  
Bisphosphate Carboxylase ◽  
Ribulose 1 ◽  
Antisense Constructs ◽  
A Cell

AbstractWe generated antisense constructs targeting two of the five Rubisco small subunit genes (OsRBCS2 and 4) which account for between 30-40% of the RBCS transcript abundance in leaf blades. The constructs were driven by a maize phosphoenolpyruvate carboxylase (PEPC) promoter known to have enriched expression in mesophyll cells (MCs). In the resulting lines leaf Rubisco protein content was reduced by between 30-50% and CO2 assimilation rate was limited under photorespiratory and non-photorespiratory conditions. A relationship between Rubisco protein content and CO2 assimilation rate was found. This was associated with a significant reduction in dry biomass accumulation and grain yield of between 37 to 70%. In addition to serving as a resource for reducing Rubisco accumulation in a cell-preferential manner, these lines allow us to characterize gene function and isoform specific suppression on photosynthesis and growth. Our results suggest that the knockdown of multiple genes is required to completely reduce Rubisco accumulation in MCs.

scholarly journals 5′ proximal sequences of a soybean ribulose-1, 5-bisphosphate carboxylase small subunit gene direct light and phytochrome controlled transcription

1987 ◽  
Vol 15 (16) ◽  
pp. 6501-6514 ◽  
Author(s):  
B.W. Shirley ◽  
S.L. Berry-Lowe ◽  
S.G. Rogers ◽  
J.S. Flick ◽  
R. Horsch ◽  
...  
Keyword(s):  
Small Subunit ◽  
Subunit Gene ◽  
Bisphosphate Carboxylase ◽  
Direct Light ◽  
Ribulose 1

Three-dimensional distribution of ribulose-1, 5-bisphosphate carboxylase/oxygemase during the early development of proplastids in dark-grown Euglena cells transferred to an inorganic medium

1990 ◽  
Vol 48 (3) ◽  
pp. 906-907
Author(s):  
Tomoko Ehara ◽  
Shuji Sumida ◽  
Tetsuaki Osafune ◽  
Eiji Hase
Keyword(s):  
Cell Suspension ◽  
Euglena Gracilis ◽  
Carbon Materials ◽  
Three Dimensional ◽  
Peripheral Region ◽  
Plastid Development ◽  
Bisphosphate Carboxylase ◽  
Inorganic Medium ◽  
Ribulose 1 ◽  
Dimensional Distribution

As shown previously, Euglena cells grown in Hutner’s medium in the dark without agitation accumulate wax as well as paramylum, and contain proplastids showing no internal structure except for a single prothylakoid existing close to the envelope. When the cells are transferred to an inorganic medium containing ammonium salt and the cell suspension is aerated in the dark, the wax was oxidatively metabolized, providing carbon materials and energy 23 for some dark processes of plastid development. Under these conditions, pyrenoid-like structures (called “pro-pyrenoids”) are formed at the sites adjacent to the prolamel larbodies (PLB) localized in the peripheral region of the proplastid. The single prothylakoid becomes paired with a newly formed prothylakoid, and a part of the paired prothylakoids is extended, with foldings, in to the “propyrenoid”. In this study, we observed a concentration of RuBisCO in the “propyrenoid” of Euglena gracilis strain Z using immunoelectron microscopy.

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