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This analysis revealed that both Pdx1 mutants can form the R5P covalent adduct as for wild type under the same conditions (Figure 1F).

Furthermore, to confirm that in the absence of the RNAi pathway epe1Δ mutants can form extended heterochromatin domains, silent chromatin was examined at a synthetic telomere.

In yeast, in the case of Erv2, it was shown that both shuttle cysteine residues were required for its function in vivo, and both single cysteine mutants can form a disulfide bond with the active-site cysteine [ 14].

These studies provide the first demonstration that Top2 mutants can form a functional heterodimer in vivo and suggest that significant cooperation can occur between defective Top2 subunits to restore in vivo function.

Our results demonstrate that in vivo yeast PS1-hp mutants can form the heterohexameric MCM complex and bind origins of DNA replication, but fail to maintain plasmid stability, indicating a defect in the transition to an active MCM complex, or an MCM complex that is defective in efficient strand separation during replication elongation.

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These data support the conclusion that the GluN1 GluN2A NMDA receptor ATD is a heterodimer and that the GluN2A K80C mutant can form a disulfide bridge with an unidentified endogenous cysteine residue in the GluN1 subunit.

Because Cdt1p is known to interact with the hexameric MCM helicase, these data indicate Mcm5p PS1-hp mutant can form the MCM complex.

Provided that minimal folding requirements are fulfilled, such as correct folding of domains involved in dimerization of LPH, it should be still considered that two different protein isoforms, such as a wild type LPH and a truncated LPH mutant can form heterodimers, which may regulate the enzymatic function.

Our results showed that mutants I432A can form both the synaptic complexes and the cleaved intermediates, but size of attR and attL have slightly difference as compared with wild-type protein.

In the present case, we speculate that the proteins encoded by the two mutant alleles can form dimers in neutral pH conditions, which also occurs between one mutant and one wild-type monomer in patients who inherit only one mutant p.R337H allele.

To test this we used the daf-8 m85); daf-8 m8577) daf-6 e1377nt daf-6 e1377rm doublelarvae constitutively (due to the daf-8 mutanton), buthat defecanve in chemosensory behavior due to daformwith improper formation of the sensory channel, preventing the olfactory neurons from contacting the environment [48], [49].

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