Award Abstract # 9727757
Structure and Function of a Novel, Modular Arabinogalactan-Protein from Tomato

NSF Org: IOS
Division Of Integrative Organismal Systems
Recipient: OHIO UNIVERSITY
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 1998 = $100,000.00
FY 1999 = $105,000.00

FY 2000 = $100,000.00
History of Investigator:
  • Allan Showalter (Principal Investigator)
    showalte@ohio.edu
  • Marcia Kieliszewski (Co-Principal Investigator)
Recipient Sponsored Research Office: Ohio University
1 OHIO UNIVERSITY
ATHENS
OH  US  45701-2979
(740)593-2857
Sponsor Congressional District: 12
Primary Place of Performance: Ohio University
1 OHIO UNIVERSITY
ATHENS
OH  US  45701-2979
Primary Place of Performance
Congressional District:
12
Unique Entity Identifier (UEI): LXHMMWRKN5N8
Parent UEI:
NSF Program(s): INTEGRATIVE PLANT BIOLOGY
Primary Program Source: app-0100 
app-0198 

app-0199 
Program Reference Code(s): 9109, 9178, 9251, BIOT, SMET
Program Element Code(s): 114500
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).

Please report errors in award information by writing to: awardsearch@nsf.gov.

Print this page

Back to Top of page