ZmPIN1a and ZmPIN1b encode two novel putative candidates for polar auxin transport and plant architecture determination of maize.
Shoot apical meristems produce organs in a highly stereotypic pattern that involves auxin. Auxin is supposed to be actively transported from cell to cell by influx (AUXIN/LIKE AUXIN proteins) and efflux (PIN-FORMED proteins) membrane carriers. Current hypotheses propose that, at the meristem surface, PIN proteins create patterns of auxin gradients that, in turn, create patterns of gene expression and morphogenesis. These hypotheses are entirely based on work in Arabidopsis (Arabidopsis thaliana). To verify whether these models also apply to other species, we studied the behavior of PIN proteins during maize (Zea mays) development. We identified two novel putative orthologs of AtPIN1 in maize and analyzed their expression pattern during development. The expression studies were complemented by immunolocalization studies using an anti-AtPIN1 antibody. Interestingly, the maize proteins visualized by this antibody are almost exclusively localized in subepidermal meristematic layers. Both tassel and ear were characterized by a compact group of cells, just below the surface, carrying PIN. In contrast to or to complement what was shown in Arabidopsis, these results point to the importance of internally localized cells in the patterning process. We chose the barren inflorescence2 (bif2) maize mutant to study the role of auxin polar fluxes in inflorescence development. In severe alleles of bif2, the tassel and the ear present altered ZmPIN1a and ZmPIN1b protein expression and localization patterns. In particular, the compact groups of cells in the tassel and ear of the mutant were missing. We conclude that BIF2 is important for PIN organization and could play a role in the establishment of polar auxin fluxes in maize inflorescence, indirectly modulating the process of axillary meristem formation and development.
Carraro
Nicola
N
Dipartimento di Agronomia Ambientale e Produzioni Vegetali, Università degli Studi di Padova Agripolis-Viale dell'Università 16, 35020 Legnaro.
Forestan
Cristian
C
Canova
Sabrina
S
Traas
Jan
J
Varotto
Serena
S
D000595:Amino Acid Sequence; D029681:Arabidopsis Proteins / Q000502:physiology; D035263:Flowering Tops / Q000254:growth & development* / Q000378:metabolism; D015870:Gene Expression; D007210:Indoleacetic Acids / Q000378:metabolism*; D026901:Membrane Transport Proteins / Q000502:physiology; D018519:Meristem / Q000378:metabolism / Q000502:physiology*; D008969:Molecular Sequence Data; D009154:Mutation; D010940:Plant Proteins / Q000235:genetics / Q000378:metabolism / Q000502:physiology*; D003313:Zea mays / Q000235:genetics / Q000254:growth & development* / Q000378:metabolism
D029681:Arabidopsis Proteins; D007210:Indoleacetic Acids; D026901:Membrane Transport Proteins; C116363:PIN1 protein, Arabidopsis; D010940:Plant Proteins