Hp. Yang et al., Diversity of Arabidopsis genes encoding precursors for phytosulfokine, a peptide growth factor, PLANT PHYSL, 127(3), 2001, pp. 842-851
Phytosulfokine-alpha (PSK-alpha), a unique plant peptide growth factor, was
originally isolated from conditioned medium of asparagus (Asparagus offici
nalis) mesophyll cell cultures. PSK-a has several biological activities inc
luding promoting plant cell proliferation. Four genes that encode precursor
s of PSK-alpha have been identified from Arabidopsis. Analysis of cDNAs for
two of these, AtPSK2 and AtPSK3, shows that both of these genes consist of
two exons and one intron. The predicted precursors have N-terminal signal
peptides and only a single PSK-alpha sequence located close to their carbox
yl termini. Both precursors contain dibasic processing sites flanking PSK,
analogous to animal and yeast prohormones. Although the PSK domain includin
g the sequence of PSK-alpha and three amino acids preceding it are perfectl
y conserved, the precursors bear very limited similarity among Arabidopsis
and rice (Oryza saliva), suggesting a new level of diversity among polypept
ides that are processed into the same signaling molecule in plants, a scena
rio not found in animals and yeast. Unnatural [serine-4]PSK-beta was found
to be secreted by transgenic Arabidopsis cells expressing a mutant of eithe
r AtPSK2 or AtPSK3 cDNAs, suggesting that both AtPSK2 and AtPSK3 encode PSK
-alpha precursors. AtPSK2 and AtPSK3 were expressed demonstrably not only i
n cultured cells but also in intact plants, suggesting that PSK-alpha may b
e essential for plant cell proliferation in vivo as well as in vitro. Overe
xpression of either precursor gene allowed the transgenic calli to grow twi
ce as large as the controls. However, the transgenic cells expressing eithe
r antisense cDNA did not dramatically decrease mitogenic activity, suggesti
ng that these two genes may act redundantly.