Pin M III gene in white pine

Details Pin M III gene in white pine Pin M III gene in white pine

1997-10-22

2001-10-23

Campbell, Eggerton A. (Department: 1653)

Chemistry: molecular biology and microbiology

Measuring or testing process involving enzymes or...

Involving nucleic acid

C536S022100

Reexamination Certificate

active

06306585

ABSTRACT:

BACKGROUND OF THE INVENTION
1. Field of the Invention
This invention relates to a gene coding for
Pin m
III which is associated with overwintering and frost hardiness of western white pine.
The invention also relates to a method of determining the frost hardiness of a conifer seedling, and to a method for determining the susceptibility of conifers to blister rust fungus.
2. Description of the Prior Art
The following disclosure refers to a plurality of literature references. The references are listed numerically at the end of this disclosure
White pine blister rust is a disease of five-needle pines, e.g. western white pine (
Pinus monticola
D. Don), eastern white pine (
Pinus strobes
L.) and sugar pine (
Pinus lambertiana
Dougl.), caused by the blister rust fungus,
Cronartium ribicola
Fisch. The fungus has five different spore stages on two unrelated hosts, white pines and Ribes species. The basidiospores are produced on Ribes in the fall and transported by wind to pine foliage, where they germinate and infect the needle via stomata and produce infection spot. Hyphae grow down the needle into the bark, causing a perennial canker which eventually kills the tree. Although some large and older trees can survive, infected younger trees almost inevitably die. We have been studying proteins involved in this host-pathogen interaction. (e.g. Ekramoddoullah and Hunt, 1993, Ref. 10). During this investigation it was observed that environmental factors also contributed to the changes in the synthesis of proteins. Plants presumably respond to signals generated by environmental stresses, e.g. low and high temperature, photoperiod, drought, salinity and are capable of responding to a varying degree to the stresses (Bohnert et al., 1995, Ref. 3). Plants also are continually exposed to numerous microorganisms but are susceptible only to a few of them. In response to both abiotic and biotic stresses, induction of several proteins in plants have been identified (Heikila et al., 1984, Ref. 16; Ort et al., 1989, Ref. 32; Hightower, 1991, Ref. 17; Stintzi et al., 1993, Ref. 41; Ekramoddoullah et al., 1995, Ref. 12; Sabehat et al., 1996, Ref. 37; Mauch et al. 1988, Ref. 28). Although functions for many of these proteins have not yet been assigned, accumulation of a group of proteins termed “pathogenesis-related” proteins (van Loon, 1985, Ref. 48; Linthorst, 1991, Ref. 25) is considered an important feature of plant defence response upon infection. Some of these proteins could be induced by either abiotic or biotic stress. For example, a protein osmotin that accumulates during adaptation of tobacco cells to osmotic stress could be induced in tobacco leaves infected with tobacco mosaic virus (Stintzi et al., 1991, Ref. 40). Genes encoding vegetative storage proteins were expressed following wounding and water deficit (Mason et al., 1991, Ref. 27). A major protein, sporamin of potato tuberous roots (Maeshima et al., 1985, Ref. 26), which is developmentally regulated, could be induced in petioles by treatment with fungal elicitors, polygalacturonic acid and chitosan (Ohto et al., 1992, Ref. 31). A family of wound induced genes in Populus shares common features with genes encoding vegetative storage proteins (Davis et al., 1993, Ref. 7) that also accumulate seasonally in poplar bark tissues (Clausen and Apel, 1991, Ref. 5)). A group of antifreeze like proteins in rye grass was shown to have amino acid sequence homology with pathogenesis-related proteins (Hon et al., 1995, Ref. 18). Recently, a sugar pine protein
Pin l
I was detected in the foliage in increasing amounts in the fall (Ekramoddoullah et al. 1995, Ref. 12). The homologue of this fall protein, named as
Pin m
III, was also identified in western white pine foliage. An 89% homology of the N-terminal amino acid sequence of
Pin m
III was found with
Pin l
I (Ekramoddoullah and Taylor, 1996, Ref. 13). The quantity of
Pin m
III in western white pine seedlings was shown to be seasonally regulated; increasing as fall progressed to a maximum in the winter months, and reducing to lowest levels in the summer months (Ekramoddoullah et al. 1995, Ref. 12).
Pin m
III has also been shown to be associated with frost hardiness of western white pine.
SUMMARY OF THE INVENTION
In order to investigate the potential anti-freeze property of Pin m III, the present inventors undertook the molecular cloning and characterization of the gene encoding
Pin m
III, which is one of the objects of this invention. An expression cDNA library from poly(A)+mRNA of pine needles was generated. The gene encoding
Pin m
III was cloned by antibody screening. BLAST search and subsequent sequence comparisons indicated
Pin m
III is a member of intracellular pathogenesis-related protein. This disclosure describes the complete sequence of the cDNA encoding
Pin m
III from western white pine, its phylogenetic relationship to other pathogenesis-related proteins, and analysis of its temporal and spatial expression. Furthermore, data are provided to show that
Pin m
III is also induced by the white pine blister rust fungus.
Accordingly, another object of the invention is to provide methods for determining frost hardiness and blister rust fungus susceptibility in a conifer by detecting the amount of the protein
Pin m
III in the conifer.
Thus according to one aspect, the invention provides a nucleic acid sequence encoding the protein
Pin m
III having the amino acid sequence of SEQ ID NO: 1.


REFERENCES:
patent: 9305164-A 6 (1993-03-01), None

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