INP1 involvement in pollen aperture formation is evolutionarily conserved and may require species-specific partners
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Oxford University Press
Materia
Arabidopsis Evolutionary analysis Exine INP1 Maize Membrane domains Plant reproduction Pollen aperture Pollen germination
Fecha
2017-11-28Referencia bibliográfica
Li, Peng; et. al. INP1 involvement in pollen aperture formation is evolutionarily conserved and may require species-specific partners. Journal of Experimental Botany, Vol. 69, No. 5 pp. 983–996, 2016 [http://hdl.handle.net/10481/50936]
Patrocinador
Funding was provided to AAD by the US National Science Foundation (MCB-1517511) and to VNSS by the Spanish Ministry of Economy and Competitiveness (CGL2015-70290-P). PL was supported by the China Scholarship Council. SB-MS was supported by the University of Granada, Spain (grant Cei BioTic). We thank the Arabidopsis Biological Resource Center (OSU) and the Maize Genetics Cooperation Stock Center (USDA/ ARS) for seed stocks, Priscila Rodriguez Garcia (OSU) for help with characterizing Arabidopsis–tomato INP1 chimeras, and Jay Hollick (OSU) for advice on all things maize.Resumen
Pollen wall exine is usually deposited non-uniformly on the pollen surface, with areas of low exine deposition
corresponding to pollen apertures. Little is known about how apertures form, with the novel Arabidopsis INP1
(INAPERTURATE POLLEN1) protein currently being the only identified aperture factor. In developing pollen, INP1
localizes to three plasma membrane domains and underlies formation of three apertures. Although INP1 homologs
are found across angiosperms, they lack strong sequence conservation. Thus, it has been unclear whether they also
act as aperture factors and whether their sequence divergence contributes to interspecies differences in aperture
patterns. To explore the functional conservation of INP1 homologs, we used mutant analysis in maize and tested
whether homologs from several other species could function in Arabidopsis. Our data suggest that the INP1 involvement
in aperture formation is evolutionarily conserved, despite the significant divergence of INP1 sequences and
aperture patterns, but that additional species-specific factors are likely to be required to guide INP1 and to provide
information for aperture patterning. To determine the regions in INP1 necessary for its localization and function, we
used fragment fusions, domain swaps, and interspecific protein chimeras. We demonstrate that the central portion of
the protein is particularly important for mediating the species-specific functionality.