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2014 ; 113
(7
): 1121-37
Nephropedia Template TP
gab.com Text
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English Wikipedia
Molecular and ultrastructural analysis of forisome subunits reveals the
principles of forisome assembly
#MMPMID24694827
Müller B
; Groscurth S
; Menzel M
; Rüping BA
; Twyman RM
; Prüfer D
; Noll GA
Ann Bot
2014[Jun]; 113
(7
): 1121-37
PMID24694827
show ga
BACKGROUND AND AIMS: Forisomes are specialized structural phloem proteins that
mediate sieve element occlusion after wounding exclusively in papilionoid
legumes, but most studies of forisome structure and function have focused on the
Old World clade rather than the early lineages. A comprehensive phylogenetic,
molecular, structural and functional analysis of forisomes from species covering
a broad spectrum of the papilionoid legumes was therefore carried out, including
the first analysis of Dipteryx panamensis forisomes, representing the earliest
branch of the Papilionoideae lineage. The aim was to study the molecular,
structural and functional conservation among forisomes from different tribes and
to establish the roles of individual forisome subunits. METHODS: Sequence
analysis and bioinformatics were combined with structural and functional analysis
of native forisomes and artificial forisome-like protein bodies, the latter
produced by expressing forisome genes from different legumes in a heterologous
background. The structure of these bodies was analysed using a combination of
confocal laser scanning microscopy (CLSM), scanning electron microscopy (SEM) and
transmission electron microscopy (TEM), and the function of individual subunits
was examined by combinatorial expression, micromanipulation and light microscopy.
KEY RESULTS: Dipteryx panamensis native forisomes and homomeric protein bodies
assembled from the single sieve element occlusion by forisome (SEO-F) subunit
identified in this species were structurally and functionally similar to
forisomes from the Old World clade. In contrast, homomeric protein bodies
assembled from individual SEO-F subunits from Old World species yielded
artificial forisomes differing in proportion to their native counterparts,
suggesting that multiple SEO-F proteins are required for forisome assembly in
these plants. Structural differences between Medicago truncatula native
forisomes, homomeric protein bodies and heteromeric bodies containing all
possible subunit combinations suggested that combinations of SEO-F proteins may
fine-tune the geometric proportions and reactivity of forisomes. CONCLUSIONS: It
is concluded that forisome structure and function have been strongly conserved
during evolution and that species-dependent subsets of SEO-F proteins may have
evolved to fine-tune the structure of native forisomes.