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Uncertainty in structures

The Journal of Cell Biology
The Rockefeller University Press
Publication Date
DOI: 10.1083/jcb1655rr3
  • Research Roundup
  • Biology


untitled Research Roundup 605 T EXT B Y N ICOLE L E B RASSEUR LEBRASN @ ROCKEFELLER . EDU Uncertainty in structures rystal structures may fit all the data, but a report from Mark DePristo and colleagues (University of Cambridge, C Models based on the crystal structure of interleukin-1� vary significantly. D eP ri st o/ El se vi er UK) warns that, for any given structure in the Protein Data Bank (PDB), there will be many other overlooked struc- tures that are equally consistent with the data. Crystallized proteins retain the ability to move around, thus making interpre- tations of diffraction data an imprecise process. Crystallographers fit their data to models that pass quality controls, but they usually report only one such model. The Cambridge group generated alternate models that fit the data for several proteins. “We found a reasonable number of structures that are surprisingly different in their finer details,” says Pollen spares all but self any plants encourage genetic diversity by preventing self- pollination. Two groups now show that this system works by protecting only an RNase that destroys self. This RNase stops the growth of genetically identical pollen tubes, but RNases that would destroy nonidentical pollen tubes are themselves degraded. The RNases are made by a part of the S -locus, a huge, intractable stretch of DNA. Although the female-specific product of the S -locus has long been known to be the S-RNase, the male-specific product (made by the pollen tube) has eluded scientists for a decade. It is now identified as a regulator of ubiquitination that seems to sentence all but self S-RNases to degradation. Through a brute force sequencing approach, Paja Sijacic, Teh-hui Kao (Penn State University), and colleagues found that the petunia pollen S -component is the SLF F-box prote

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