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Analysis of these mutants indicates that greater than 5% of Smn protein is required for normal development.

Furthermore, the dramatic loss of function in these mutants indicates the three-way junction is a critical element in conferring Xrn1 resistance and is likely the central element around which the structure organizes.

The rescue of Nup116-C toxicity by these mutants indicates that the substitutions do not significantly affect activity or abundance of the full-length Snl1-L required to suppress the toxicity.

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Interestingly, some of these mutants indicate that the formation of primary-, seminal-, crown- and lateral roots is regulated by alternative root-type-specific pathways.

A hypothetical model of MutY-mediated formation of a short ISR is shown in Fig. 4. The inactivation of three other predicted BER glycosylase genes, magIII, ung, and nth, had no significant effect on the import length, and ISR were still observed in these mutants, indicating that neither of them is essential for ISR formation.

We successfully constructed seven sRNA-deleted mutants, and proteomic analysis performed on three of these mutants indicated that the corresponding sRNAs are likely to be involved in various physiological pathways.

The first description of these mutants indicated a precocious seam cell terminal differentiation that leads to the formation of adult-specific alae during the third molt (Abrahante et al. 1998; Jeon et al. 1999).

Notably, the wavelength maxima of the Soret peaks for both of these mutants indicated the presence of heme iron in the characteristically ferrous (Fe2+) state (418 nm for W118A and 419 nm for N128A/M130A) and remained unchanged upon the addition of reducing agent.

In vitro cGAMP activity assay and HPLC analysis of these mutants indicated that the HD-GYP domain is absolutely essential for the PDE activity of all three V-cGAPs; however, mutation of the N-terminal HD domain of VCA0681 (M1) showed a minor effect.

Our analyses of these mutants indicate that the integrity of both the Spt16-D and Spt16-M domains not only are required for SRG1 transcription-dependent nucleosome assembly and SER3 repression but also are more broadly required for transcription-coupled nucleosome occupancy at highly transcribed genes.

However, no evidence of infection was detected in embryo tissues from eggs infected with the mutants indicating that these viruses are unable to cross the chorio-allantoic membrane, a typical feature of low pathogenic avian influenza viruses (LPAIV).

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