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At postnatal day 14, mutants were characterized by dramatic hypomyelination (Fig. 2a, c), reduction of CC1+/OLIG2+ OLs (Fig. 2b, d), and precocious mortality (Fig. 2e).

These mutants were characterized with respect to their antifreeze activity and Ca2+-binding properties.

Representative mutants were characterized by the neutralization assays as described above.

All mutants were characterized by great reduction in kinase activity toward Rb-GST fusion protein as assayed in vitro [22], [23].

The mutants were characterized in vivo using the model organism S. cerevisiae as it affords a genetic background that can be readily manipulated.

The genomic DNAs of the mutants were characterized by PCR (Materials and Methods) and the junctions between the T-DNAs and the gene were sequenced.

Interestingly, regardless of the compartment of protein stress origin, all mutants experience the increase in cytosolic Hsp90 levels, relative to the WT (Fig. 1a, Supplementary Fig. S1). Figure 1: Chaperone deletion mutants are characterized by increased proteotoxicity and repressed mitochondrial activity.

Crl4 and Osgnom1 mutants are characterized by an absence of crown roots and a reduced number of lateral roots.

Crl1 and arl1 mutants are characterized by a total absence of crown root initiation and a reduced number of lateral roots.

Although these mutants are characterized by semi-dwarf phenotype, all of them are sensitive to GA3 [ 18].

In this study the transcriptome of S39006 WT and the hfq and rsmA mutants was characterized and differential expression determined.