J. Arines et al., PROTEIN-PATTERNS AND SUPEROXIDE-DISMUTASE ACTIVITY IN NONMYCORRHIZAL AND ARBUSCULAR MYCORRHIZAL PISUM-SATIVUM L PLANTS, Plant and soil, 166(1), 1994, pp. 37-45
There are few reports in relation to the role of specific proteins in
the mycorrhizal symbiosis. Among the changes in the protein expression
as a consequence of the arbuscular mycorrhizal symbiosis, only one ca
se related to changes in superoxide dismutase (SOD; EC 1.15.1.1) activ
ity has been reported in the red clover- Glomus mosseae symbiosis. In
this paper, the symbiotic system formed by a leguminous plant, Pisum s
ativum, and the fungus Glomus mosseae is studied in terms of protein p
atterns and SOD activity in both mycorrhizal and non-mycorrhizal roots
. Our results show that among the differential polypeptides separated
by SDS-PAGE, one with a molecular weight of 32.0 kDa, and a protein wi
th an isoelectric point of pI 4.9 appeared strongly expressed in mycor
rhizal roots. A partial purification of the related polypeptide could
be achieved by DEAE-cellulose chromatography. A higher SOD activity wa
s also detected in mycorrhizal pea roots, although both mycorrhizal an
d non-mycorrhizal roots showed the same isoenzymatic pattern for SODs:
two Mn-SODs (I and II) and two Cu,Zn-SODs (I and II) were detected, C
u,Zn-SOD I being the most abundant isozyme in both types of roots. A s
imilar pattern of SOD isozymes (Mn-SODs I and II, and Cu,Zn-SODs I and
II) was also found in nodules of mycorrhizal and non-mycorrhizal pea
roots. However, in nodules Mn-SOD II was the main isozyme. The bacteri
al nature of this isozyme is postulated in this report.