AtPNP-A is a systemically mobile natriuretic peptide immunoanalogue with a role in Arabidopsis thaliana cell volume regulation.
Cellular and physiological evidence suggests the presence of a novel class of systemically mobile plant molecules that are recognized by antibodies against vertebrate atrial natriuretic peptides (ANPs). In order to characterize the function of these immunoanalogues we have expressed the full-length recombinant (AtPNP-A[1-126]) and demonstrate that this molecule induces osmoticum-dependent H(2)O uptake into protoplasts at nanomolar concentrations and thus affects cell volume. A similar response is also seen with a recombinant that does not contain the signal peptide (AtPNP-A[26-126]) as well as a short domain (AtPNP-A[33-66]) that shows homology to the vertebrate peptide. Taken together, these findings suggest that AtPNP-A has an important and systemic role in plant growth and homeostasis.
Morse
Monique
M
University of the Western Cape, Department of Biotechnology, Private Bag X17, 7535, Bellville, South Africa.
Pironcheva
Ganka
G
Gehring
Chris
C
D000595:Amino Acid Sequence; D017360:Arabidopsis / Q000166:cytology* / Q000187:drug effects / Q000235:genetics / Q000378:metabolism; D029681:Arabidopsis Proteins / Q000494:pharmacology* / Q000502:physiology*; D048429:Cell Size / Q000187:drug effects* / Q000502:physiology; D003513:Cycloheximide / Q000494:pharmacology; D008969:Molecular Sequence Data; D009997:Osmotic Pressure; D010446:Peptide Fragments / Q000494:pharmacology*; D017434:Protein Structure, Tertiary; D011523:Protoplasts / Q000166:cytology / Q000187:drug effects / Q000502:physiology; D011994:Recombinant Proteins / Q000235:genetics / Q000378:metabolism / Q000494:pharmacology; D017386:Sequence Homology, Amino Acid; D013012:Sorbitol / Q000494:pharmacology
D029681:Arabidopsis Proteins; C464762:PNP-A protein, Arabidopsis; D010446:Peptide Fragments; D011994:Recombinant Proteins; D013012:Sorbitol; D003513:Cycloheximide