Characterisation and high-resolution distribution of a matrix attachment region-binding protein (MFP1) in proliferating cells of onion

Citation
R. Samaniego et al., Characterisation and high-resolution distribution of a matrix attachment region-binding protein (MFP1) in proliferating cells of onion, PLANTA, 212(4), 2001, pp. 535-546
Citations number
35
Categorie Soggetti
Plant Sciences","Animal & Plant Sciences
Journal title
PLANTA
ISSN journal
00320935 → ACNP
Volume
212
Issue
4
Year of publication
2001
Pages
535 - 546
Database
ISI
SICI code
0032-0935(200103)212:4<535:CAHDOA>2.0.ZU;2-4
Abstract
The first matrix attachment region (MAR)-binding protein sequenced in plant s, MFP1, has been characterised in two dicot species. Based on their antige nic relationship, we report here the conservation of MFP1-like proteins in proliferating root cells of onion (Allium cepa L). Two MFP1-like proteins w ith different molecular masses and solubilities were detected. The most abu ndant was a 90-kDa basic protein, presenting several separate spots in two- dimensional blots. The MFP1 was partially soluble and, similar to the proli ferating cell nuclear antigen (PCNA)-labelled replication factories in the nucleus and nuclear matrix, was localised at discrete foci as detected by c onfocal microscopy. High-resolution immunolocalisation of MFP1 by electron microscopy identified the foci as nuclear structures, some of them containi ng PCNA, which are ultrastructurally similar to the replication factories d escribed in animal cells. Our data provide the first report on MFP1-like pr oteins in the Alliaceae. In addition, we present evidence of the presence o f AcMFP1 in the putative replication factories.