We have long been involved in elucidating the metabolic pathways for both biosynthesis and degradation of several acyclic sugar alcohols, e.g., sorbitol and mannitol, and determining the characteristics and tissue, cell, and subcellular locations of those enzymes involved in these pathways. Enzyme identification and characterization currently includes study of regulatory mechanisms at both the protein and gene level. We have, for example, cloned and sequenced the gene for mannose 6-phosphate reductase, a key step in mannitol biosynthesis, and are now investigating those factors involved in its regulation. For our work on mannitol metabolism in plants we initially used MALDI-MS to verify less accurate molecular weight determinations of the enzyme mannose 6-phosphate reductase (M6PR). Following gene cloning, MALDI-MS also confirmed clonal identity by allowing a comparison of the molecular weights of the clonally expressed bacterial and the native plant enzymes. The importance of this work relates to plant stress physiology. We are very interested in developing an understanding of the mechanisms by which plants tolerate abiotic stress, environmental extremes such as salinity, drought, and temperature, especially since several of these mechanisms may be related to the capacity of some plants to synthesize compatible solutes like the acyclic sugar alcohols. Accordingly, we have been looking at how certain abiotic stresses regulate sugar alcohol metabolism, storage, and transport, and how these compounds may accumulate in response to exposure to stress. M6PR along with several similar enzymes in other plants is a key step in acyclic sugar alcohol biosynthesis. Engineering plants with a gene for M6PR can have important implications for developing plants with improved stress tolerance.

Agency
National Institute of Health (NIH)
Institute
National Center for Research Resources (NCRR)
Type
Biotechnology Resource Grants (P41)
Project #
3P41RR000480-28S1
Application #
6258833
Study Section
Project Start
1997-06-01
Project End
1999-11-30
Budget Start
1998-10-01
Budget End
1999-09-30
Support Year
28
Fiscal Year
1999
Total Cost
Indirect Cost
Name
Michigan State University
Department
Type
DUNS #
193247145
City
East Lansing
State
MI
Country
United States
Zip Code
48824
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Chen, H M; Sood, R; Hosmane, R S (1999) An efficient, short synthesis and potent anti-hepatitis B viral activity of a novel ring-expanded purine nucleoside analogue containing a 5:7-fused, planar, aromatic, imidazo[4,5-e][1,3]diazepine ring system. Nucleosides Nucleotides 18:331-5
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Agasimundin, Y S; Mumper, M W; Hosmane, R S (1998) Inhibitors of glycogen phosphorylase b: synthesis, biochemical screening, and molecular modeling studies of novel analogues of hydantocidin. Bioorg Med Chem 6:911-23
Hosmane, R S; Peri, S P; Bhadti, V S et al. (1998) Bis[2-(4-carboxyphenoxy)carbonylethyl]phosphinic acid (BCCEP): a novel affinity reagent for the beta-cleft modification of human hemoglobin. Bioorg Med Chem 6:767-83
Rajappan, V P; Hosmane, R S (1998) Analogues of azepinomycin as inhibitors of guanase. Nucleosides Nucleotides 17:1141-51
Hosmane, R S; Hong, M (1997) How important is the N-3 sugar moiety in the tight-binding interaction of coformycin with adenosine deaminase? Biochem Biophys Res Commun 236:88-93
Lopez-Lara, I M; Orgambide, G; Dazzo, F B et al. (1993) Characterization and symbiotic importance of acidic extracellular polysaccharides of Rhizobium sp. strain GRH2 isolated from acacia nodules. J Bacteriol 175:2826-32
Watson, J T; Kayganich, K (1989) Novel sample preparation for analysis by electron capture negative ionization mass spectrometry. Biochem Soc Trans 17:254-7
Kassel, D B; Kayganich, K A; Watson, J T et al. (1988) Utility of ion source pretreatment with chlorine-containing compounds for enhanced performance in gas chromatography/negative ionization mass spectrometry. Anal Chem 60:911-7

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