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Exact(4)
The s1 and s2 mutants map to SesA.
The SNP analysis revealed that 22 mutants map to only five chromosomal regions; only mr37 showed no Mendelian inheritance of the trait.
We show that in a collection of 136 randomly selected Ctf mutants, >65% of mutants map to 13 genes, 12 of which are involved in sister chromatid cohesion and/or kinetochore function.
Although such hypotheses are currently beyond experimental proof, it is interesting to note that several, structurally unexplained superactivity mutants map to this central sequence (for example, mjA' D816-N; Q817-S/T/C/K and V819-K Figure 2A[ 20]), and that this region is also exceptionally tolerant to radical twisting of the α-helical axis induced by deletions of two-amino acid segments.
Similar(56)
The mutants mapped to similar genetic loci were tested.
Several of the Group 2 and Group 3 mutants mapped to the same functional group or pathways as Group 1 mutants.
Group 2 and Group 3 mutants that did not overlap with Group 1 mutants mapped to pathways involved in DNA replication, LPS synthesis, energy metabolism, and siderophore hydrolysis suggesting that genes within Group 2 and Group 3 are not important for the transition of classical bacteria into L-form colonies but rather for improved L-form colony growth.
Rather than complete the allelism tests we decided to undertake preliminary genetic mapping to ascertain whether these four mutants mapped to the sites of known loci.
However clinically relevant proteins tend to be key targets for structural studies, and as more structures become available, the number of mutants mapped to structure will increase, improving the coverage of our method.
While there is certainly ascertainment bias in this analysis, in the characterization of ENU mutants mapped to loci where known candidates reside, presumptively causal sequence variants can usually be found in coding regions or splice sites (e.g., [ 8]).
Residues that are invariant amongst Doc1/Apc10 sequences, including a temperature-sensitive mitotic arrest mutant, map to a β-sheet region of the molecule, whose counterpart in galactose oxidase, the coagulation factor C2 domains and XRCC1, mediate bio-molecular interactions.
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