
NSF Org: |
IOS Division Of Integrative Organismal Systems |
Recipient: |
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Initial Amendment Date: | February 3, 1998 |
Latest Amendment Date: | May 25, 2001 |
Award Number: | 9727757 |
Award Instrument: | Continuing Grant |
Program Manager: |
Sharman D. O'Neill
IOS Division Of Integrative Organismal Systems BIO Directorate for Biological Sciences |
Start Date: | April 1, 1998 |
End Date: | March 31, 2002 (Estimated) |
Total Intended Award Amount: | $300,000.00 |
Total Awarded Amount to Date: | $305,000.00 |
Funds Obligated to Date: |
FY 1999 = $105,000.00 FY 2000 = $100,000.00 |
History of Investigator: |
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Recipient Sponsored Research Office: |
1 OHIO UNIVERSITY ATHENS OH US 45701-2979 (740)593-2857 |
Sponsor Congressional District: |
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Primary Place of Performance: |
1 OHIO UNIVERSITY ATHENS OH US 45701-2979 |
Primary Place of
Performance Congressional District: |
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Unique Entity Identifier (UEI): |
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Parent UEI: |
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NSF Program(s): | INTEGRATIVE PLANT BIOLOGY |
Primary Program Source: |
app-0198 app-0199 |
Program Reference Code(s): |
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Program Element Code(s): |
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Award Agency Code: | 4900 |
Fund Agency Code: | 4900 |
Assistance Listing Number(s): | 47.074 |
ABSTRACT
9727757; PI -- Showalter
Arabinogalactan-proteins (AGPs) are a family of hydroxyproline-rich
glycoproteins which are widely distributed in plants. AGPs are found in
intercellular spaces, cell walls, and plasma membranes and implicated to
play important roles in growth and development. This proposal focuses on a
putative plasma membrane AGP, LeAGP-1, deduced from tomato DNA clones which
demonstrate developmental and organ-specific regulation. The clones
predict a novel, modular AGP comprised of an N-terminal signal peptide, a
central classical AGP domain sandwiching a basic subdomain, and C-terminal
putative transmembrane domain. Our working hypotheses are that LeAGP-1
represents a plasma membrane AGP and that it functions in establishing
connections and mediating adhesion to the cell wall, analogous to animal
cell adhesion molecules. The PIs will test these hypotheses and address
structure and function of LeAGP-1 by: 1) isolating and biochemically
characterizing LeAGP-1 from tomato cell cultures to provide structural
information and material for functional characterization, 2)
immunolocalizing LeAGP-1 in cultured cells, stems, and flowers and in
plasmolyzed cells demonstrating zones of adhesion between the membrane and
wall, and 3) functionally characterizing LeAGP-1 at the molecular level
(tests for intermolecular crosslinking) and whole plant level (LeAGP-1
antisense suppression/sense cosuppression in transgenic plants).
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