7 research outputs found

    Coefficient analysis and association between morpho-agronomical characters in common bean (Phaseolus vulgaris L.)

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    Pulses are important food sources for human consumption. In an attempt to study the associations between common bean (Phaseolus vulgaris L.) morpho-agronomical traits, twelve genotypes and inbred lines were evaluated in a randomized complete block design (RCBD) with three replications in 2010- 2011 crop season. Seed yield and 20 other morpho-agronomic characters were recorded. Analysis of variance (ANOVA) revealed a significant (p ≤ 0.01) difference among genotypes with respect to almost all traits. Correlation analysis demonstrated that seed yield had a strong positive correlation with both seed number per plant and seed number per pod, suggesting the usefulness of these traits in common bean breeding programs. Step-wise regression analysis pointed out that the pod weight, seed number per pod and 100 seed weight contributed to the seed yield prediction, whereas other traits did not contributed to the seed yield prediction. These traits explained almost 99% of total seed yield variations. Path analysis showed that the maximum direct and positive effect was related to pod weight. Furthermore, factor analysis revealed that four factors, explained almost 71% of the total variance. The results of this research showed that biologic yield, pod weight, straw weight, number of pod per plant and seed number per plant were the most closely related traits to the seed yield

    Expression of an engineered granule-bound Escherichia coli glycogen branching enzyme in potato results in severe morphological changes in starch granules

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    The Escherichia coli glycogen branching enzyme (GLGB) was fused to either the C- or N-terminus of a starch-binding domain (SBD) and expressed in two potato genetic backgrounds: the amylose-free mutant (amf) and an amylose-containing line (Kardal). Regardless of background or construct used, a large amount of GLGB/SBD fusion protein was accumulated inside the starch granules, however, without an increase in branching. The presence of GLGB/SBD fusion proteins resulted in altered morphology of the starch granules in both genetic backgrounds. In the amf genetic background, the starch granules showed both amalgamated granules and porous starch granules, whereas in Kardal background, the starch granules showed an irregular rough surface. The altered starch granules in both amf and Kardal backgrounds were visible from the initial stage of potato tuber development. High-throughput transcriptomic analysis showed that expression of GLGB/SBD fusion protein in potato tubers did not affect the expression level of most genes directly involved in the starch biosynthesis except for the up-regulation of a beta-amylase gene in Kardal background. The beta-amylase protein could be responsible for the degradation of the extra branches potentially introduced by GLGB

    Fusion proteins comprising the catalytic domain of mutansucrase and a starch-binding domain can alter the morphology of amylose-free potato starch granules during biosynthesis

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    It has been shown previously that mutan can be co-synthesized with starch when a truncated mutansucrase (GtfICAT) is directed to potato tuber amyloplasts. The mutan seemed to adhere to the isolated starch granules, but it was not incorporated in the starch granules. In this study, GtfICAT was fused to the N- or C-terminus of a starch-binding domain (SBD). These constructs were introduced into two genetically different potato backgrounds (cv. Kardal and amf), in order to bring GtfICAT in more intimate contact with growing starch granules, and to facilitate the incorporation of mutan polymers in starch. Fusion proteins of the appropriate size were evidenced in starch granules, particularly in the amf back- ground. The starches from the various GtfICAT/ SBD transformants seemed to contain less mutan than those from transformants with GtfICAT alone, suggesting that the appended SBD might inhibit the activity of GtfICAT in the engineered fusion proteins. Scanning electron microscopy showed that expression of SBD-GtfICAT resulted in alterations of granule morphology in both genetic backgrounds. Surprisingly, the amf starches con- taining SBD-GtfICAT had a spongeous appearance, i.e., the granule surface contained many small holes and grooves, suggesting that this fusion protein can interfere with the lateral interactions of amylopectin sidechains. No differences in phys- ico-chemical properties of the transgenic starches were observed. Our results show that expression of granule-bound and ‘‘soluble’’ GtfICAT can affect starch biosynthesis differently
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