Isolated spinach ribulose-1,5-bisphosphate carboxylase/oxygenase large subunit .sup..epsilon. N-methyltransferase and method of inactivating ribulose-1,5-bisphosphatase carboxylase/oxygenase large subunit .sup..epsilon. N-methyltransferase activity
Abstract
The gene sequence for ribulose-1,5-bisphosphate carboxylase/oxygenase (Rubisco) large subunit (LS) .sup..epsilon. N-methyltransferase (protein methylase III or Rubisco LSMT) from a plant which has a des(methyl) lysyl residue in the LS is disclosed. In addition, the full-length cDNA clones for Rubisco LSMT are disclosed. Transgenic plants and methods of producing same which have the Rubisco LSMT gene inserted into the DNA are also provided. Further, methods of inactivating the enzymatic activity of Rubisco LSMT are also disclosed.
- Inventors:
-
- (Lexington, KY)
- Publication Date:
- Research Org.:
- University of Kentucky Research Foundation (Lexington, KY)
- OSTI Identifier:
- 872316
- Patent Number(s):
- US 5908972
- Assignee:
- University of Kentucky Research Foundation (Lexington, KY) ORO
- DOE Contract Number:
- FG05-92ER26075
- Resource Type:
- Patent
- Country of Publication:
- United States
- Language:
- English
- Subject:
- isolated; spinach; ribulose-1; 5-bisphosphate; carboxylase; oxygenase; subunit; epsilon; n-methyltransferase; method; inactivating; 5-bisphosphatase; activity; sequence; rubisco; protein; methylase; iii; lsmt; plant; methyl; lysyl; residue; disclosed; addition; full-length; cdna; clones; transgenic; plants; methods; producing; inserted; dna; provided; enzymatic; cdna clones; cdna clone; rubisco lsmt; transgenic plants; protein methylase; methylase iii; full-length cdna; n-methyltransferase activity; enzymatic activity; transgenic plant; spinach ribulose-1; inactivating ribulose-1; isolated spinach; /800/435/999/
Citation Formats
Houtz, Robert L. Isolated spinach ribulose-1,5-bisphosphate carboxylase/oxygenase large subunit .sup..epsilon. N-methyltransferase and method of inactivating ribulose-1,5-bisphosphatase carboxylase/oxygenase large subunit .sup..epsilon. N-methyltransferase activity. United States: N. p., 1999.
Web.
Houtz, Robert L. Isolated spinach ribulose-1,5-bisphosphate carboxylase/oxygenase large subunit .sup..epsilon. N-methyltransferase and method of inactivating ribulose-1,5-bisphosphatase carboxylase/oxygenase large subunit .sup..epsilon. N-methyltransferase activity. United States.
Houtz, Robert L. Fri .
"Isolated spinach ribulose-1,5-bisphosphate carboxylase/oxygenase large subunit .sup..epsilon. N-methyltransferase and method of inactivating ribulose-1,5-bisphosphatase carboxylase/oxygenase large subunit .sup..epsilon. N-methyltransferase activity". United States. https://www.osti.gov/servlets/purl/872316.
@article{osti_872316,
title = {Isolated spinach ribulose-1,5-bisphosphate carboxylase/oxygenase large subunit .sup..epsilon. N-methyltransferase and method of inactivating ribulose-1,5-bisphosphatase carboxylase/oxygenase large subunit .sup..epsilon. N-methyltransferase activity},
author = {Houtz, Robert L.},
abstractNote = {The gene sequence for ribulose-1,5-bisphosphate carboxylase/oxygenase (Rubisco) large subunit (LS) .sup..epsilon. N-methyltransferase (protein methylase III or Rubisco LSMT) from a plant which has a des(methyl) lysyl residue in the LS is disclosed. In addition, the full-length cDNA clones for Rubisco LSMT are disclosed. Transgenic plants and methods of producing same which have the Rubisco LSMT gene inserted into the DNA are also provided. Further, methods of inactivating the enzymatic activity of Rubisco LSMT are also disclosed.},
doi = {},
journal = {},
number = ,
volume = ,
place = {United States},
year = {1999},
month = {1}
}
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