First, the let-23(n1045) hypomorphic mutant, which affects an EGF receptor, was crossed with ndk-1 ok314 ndk-1 ok314
First, we observed that the FLAG-tagged K498A substitution mutant, which affects an ATP binding residue and abolishes the ATPase activity of UPF1 (Cheng et al., 2007) and is hyperphosphorylated displayed similar binding to T7-tagged DHX34 as the wild-type FLAG-UPF1 protein.
By transferring the mutant mtDNA in transmitochondrial cytoplasmic hybrid (cybrid) cells we established the pathogenic role of this mutation, which affects CI function in homoplasmic mutant cybrids.
We propose that such mutants mark alternatively spliced exons whereas mutants which affect all three phenotypes (dpolv) are located in constitutive exons.
A chloroplast copper transporter was identified by a complementation group of NPQ-deficient mutants, which affect electron transport by restricting the supply of copper for holoplastocyanin assembly in the thylakoid lumen [8].
In fact, it has been proposed that the effects observed in mouse Dax1 mutants, which affect normal granulosa cell organization around oocytes in females, could be functionally related to the defects in Sertoli cell support of germ cells observed in males [70].
Focusing on the Batumi and Roo transposons, we observed that primary piRNAs were preferentially lost in vret mutants, almost exclusively leaving 10 nt offset 'ping-pong' pairs in vret mutant ovaries (Fig. 6F,G); this is similar to observations in armi and piwi mutants, and in contrast to aub mutants, which affect 'ping-pong' amplification (Fig. 6F) (Malone et al., 2009; Olivieri et al., 2010).
Moreover, the mutants defective in iron acquisition such as Δftr1 as well as copper transporter mutant Δccc2, which affects the high affinity iron uptake in Candida also showed hypersensitivity without the addition of BPS (Fig. 2B).
The kto/med12 mutant zebrafish, which affects the Mediator component Med12, causes specific loss of rhombomere boundary cells even though segmentation of the hindbrain takes place at least in part.
The premature aging disorder, Hutchinson-Gilford progeria syndrome (HGPS), is caused by mutant lamin A, which affects the nuclear scaffolding.
Although wild-type GalT-II is expressed in the Golgi, the mutant enzyme (p.Met1?), which affects the initiation codon, c.1A>G, is located in the cytoplasm and nucleus [ 29], suggesting that mislocalization of the mutant protein may cause GalT-II dysfunctions.
