PMID- 24694827
OWN - NLM
STAT- MEDLINE
DCOM- 20150115
LR  - 20240109
IS  - 1095-8290 (Electronic)
IS  - 0305-7364 (Print)
IS  - 0305-7364 (Linking)
VI  - 113
IP  - 7
DP  - 2014 Jun
TI  - Molecular and ultrastructural analysis of forisome subunits reveals the 
      principles of forisome assembly.
PG  - 1121-37
LID - 10.1093/aob/mcu036 [doi]
AB  - 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.
CI  - (c) The Author 2014. Published by Oxford University Press on behalf of the Annals 
      of Botany Company. All rights reserved. For Permissions, please email: 
      journals.permissions@oup.com.
FAU - Muller, Boje
AU  - Muller B
AD  - Institute of Plant Biology and Biotechnology, University of Munster, Schlossplatz 
      8, 48143 Munster, Germany.
FAU - Groscurth, Sira
AU  - Groscurth S
AD  - Fraunhofer Institute for Molecular Biology and Applied Ecology IME, Schlossplatz 
      8, 48143 Munster, Germany.
FAU - Menzel, Matthias
AU  - Menzel M
AD  - Fraunhofer Institute for Mechanics and Materials IWM, Walter-Hulse-Strasse 1, 
      06120 Halle, Germany.
FAU - Ruping, Boris A
AU  - Ruping BA
AD  - Institute of Plant Biology and Biotechnology, University of Munster, Schlossplatz 
      8, 48143 Munster, Germany.
FAU - Twyman, Richard M
AU  - Twyman RM
AD  - TRM Ltd, PO Box 93, York YO43 3WE, UK.
FAU - Prufer, Dirk
AU  - Prufer D
AD  - Institute of Plant Biology and Biotechnology, University of Munster, Schlossplatz 
      8, 48143 Munster, Germany Fraunhofer Institute for Molecular Biology and Applied 
      Ecology IME, Schlossplatz 8, 48143 Munster, Germany dpruefer@uni-muenster.de.
FAU - Noll, Gundula A
AU  - Noll GA
AD  - Institute of Plant Biology and Biotechnology, University of Munster, Schlossplatz 
      8, 48143 Munster, Germany.
LA  - eng
SI  - GENBANK/KJ439756
SI  - GENBANK/KJ439757
PT  - Journal Article
PT  - Research Support, Non-U.S. Gov't
DEP - 20140402
PL  - England
TA  - Ann Bot
JT  - Annals of botany
JID - 0372347
RN  - 0 (Plant Proteins)
SB  - IM
MH  - Amino Acid Sequence
MH  - Computational Biology
MH  - Fabaceae/chemistry/*genetics/metabolism
MH  - Microscopy, Confocal
MH  - Microscopy, Electron, Scanning
MH  - Microscopy, Electron, Transmission
MH  - Molecular Sequence Data
MH  - Phylogeny
MH  - Plant Proteins/*genetics/metabolism/*ultrastructure
MH  - Sequence Alignment
PMC - PMC4030808
OTO - NOTNLM
OT  - Canavalia gladiata
OT  - Dipteryx panamensis
OT  - Fabaceae
OT  - Forisome evolution
OT  - Lotus japonicus
OT  - Medicago truncatula
OT  - Papilionoideae
OT  - Pisum sativum
OT  - SEO
OT  - Vicia faba
OT  - macromolecular assembly
OT  - papilionoid legumes
OT  - sieve element occlusion gene family
OT  - structural phloem protein
EDAT- 2014/04/04 06:00
MHDA- 2015/01/16 06:00
PMCR- 2015/06/01
CRDT- 2014/04/04 06:00
PHST- 2014/04/04 06:00 [entrez]
PHST- 2014/04/04 06:00 [pubmed]
PHST- 2015/01/16 06:00 [medline]
PHST- 2015/06/01 00:00 [pmc-release]
AID - mcu036 [pii]
AID - 10.1093/aob/mcu036 [doi]
PST - ppublish
SO  - Ann Bot. 2014 Jun;113(7):1121-37. doi: 10.1093/aob/mcu036. Epub 2014 Apr 2.