The biochemical and molecular basis of the defense in a mild tolerant (ICPL-332) and susceptible (ICPL-87) cultivars of pigeon pea (Cajanus cajan) due to Helicoverpa. armigera infestation was studied. We found that feeding by the larvae generated H 2 O 2 in a localized manner and activity was observed upto 12 h (hrs) of with a sharp decline within 24 h. Similarly, PPO activity was also detected till 12 h of treatment, which decreased after 24 h of feeding by larvae. The activity of trypsin inhibitor was detected in all the treatments when assayed at 12 and 24 h after larval feeding. The expression of defense genes like the Pre-hevein-like protein PR-4 precursor (PR-4), protease inhibitor/seed storage/LTP family protein (Ltp) were significantly up-regulated in ICPL-332 upon infestation after 12 h as compared to ICPL-87, whereas the endo 1, 4-β-glucanase (Kor-1) gene was expressed in both the cultivars after 24 h of infestation. Both the cultivars varied with respect to the induction of defense-related genes during larval feeding, both the PR-4 and Ltp genes appeared to be important for defense against H. armigera in pigeon pea. Thus, the present study revealed an insight of herbivore-induced biochemical and molecular changes in pigeon pea.

Background: Chickpea is a widely grown legume in India, Australia, Canada, and Mediterranean regions. Seeds of chickpea are good source of protein for both human and animals. Wild relatives of chickpea (Cicer arietinum) are the potential gene pool for crop improvement; however, very little information is available on the seed proteome of these wild chickpeas. Objective: We aimed to analyze the seed proteome profiles of three wild relatives of chickpea, Cicer bijugum, Cicer judaicum and Cicer microphyllum along with two cultivated varieties JG11 and DCP 92/3. Method: Total seed proteins were extracted using various extraction buffers for 2-D gel electrophoresis. Protein separated in a 2-D gels were subjected to image analyses, differentially expressed proteins were extracted from the gels and identified by the MALDI TOF/TOF. Seed protease inhibitors were analysed biochemically. Results: We have standardized the 2-D gel electrophoresis method and separated seed proteins using the modified method. We identified a large number (400) of protein proteins which were differentially expressed in cultivated and wild type species of chickpea. A comparative analysis between C. bijugum and JG 11 revealed the presence of 9 over-expressed and 22 under-expressed proteins, while the comparison between C. bijugum with DCP 92/3 showed 8 over-expressed and 18 under-expressed proteins. Similarly, comparative analysis between C. microphyllum with DCP 92/3 showed 8 over-expressed proteins along with 22 under-expressed proteins, while the comparative study of C. microphyllum with JG11 displayed 9 over-expressed and 24 under-expressed proteins. We also compared C. judaicum with DCP 92/3 which revealed 15 overexpressed and 11 under-expressed proteins. On the other hand, the comparative analysis of C. judaicum with JG11 showed 10 over-expressed proteins, while the numbers of under-expressed proteins were 14. Among the differentially expressed protein proteins, 19 proteins were analyzed by the MS/MS, and peptides were identified using the MASCOT search engine. In teh wild relatives the differtially expressed proteins are phosphatidylinositol 4-phosphate 5- kinase, β-1-6 galactosyltransferase, RNA helicase, phenyl alanine ammonia lyase 2, flavone 3’-0-methyl transferase, Argonaute 2, Myb related protein, Tubulin beta-2 chain and others. The most important one was legumin having α- amylase inhibition activity which was up regulated in C. bijugum. We also studied the activity of protease inhibitor (trypsin and α- amylase inhibitors) in these seed lines which showed differential activity of protease inhibitors. The highest trypsin and α- amylase inhibition was observed in C. judaicum and C. bijugum, respectively. Conclusion: The differentially expressed proteins of wild relatives of chickpea appeared to be involved in various metabolic pathways. The study provides us information about the differences in the seed proteome of these wild species and cultivated varieties for the first time.

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We introduce a new polynomial whose zero set forms a unique range set for meromorphic function with 11 elements under relaxed sharing hypothesis. 195 196 ABHIJIT BANERJEE AND SANTANU DHARQuestion A. Can one find two (or possibly even one) finite sets S j (j = 1, 2) such that any two non-constant entire functions f and g satisfying E(S j , f ) = E(S j , g) for j = 1, 2 must be identical?Gradually the research to find the possible answer of Question A corresponding to meromorphic functions has become one of the most prominent branches of the uniqueness theory. Later on many analogous questions were raised by many researchers pertinent to their investigations. It is needless to say that investigations for possible answers of these questions have enriched the uniqueness theory vis-à-vis the value distribution theory. Meanwhile, Gross and Yang [9] (see also [13]) introduced the new idea of a unique range set for meromorphic functions (URSM, in brief) in the following manner.Definition 1.1 (see [9]). A set S such that for any two non-constant entire (meromorphic) functions f and g the condition E(S, f ) = E(S, g) implies f ≡ g is called a unique range set of entire (meromorphic) functions. We call it URSE (URSM) in short.Recently the definition of unique range sets have been generalized in [4] as follows.Definition 1.2 (see [4]). A set S is called a URSM p) (URSE p) ) if for any two non-constant meromorphic (entire) functions f and g the equality E p) (S, f ) = E p) (S, g) implies f ≡ g.