No abstract

Chromosome segregation during mitosis requires assembly of the kinetochore complex at the centromere. Key to kinetochore assembly is the specific recognition of the histone variant CENP-A in the centromeric nucleosome by centromere protein C (CENP-C). We have defined the determinants of this recognition mechanism and discovered that CENP-C binds a hydrophobic region in the CENP-A tail and docks onto the acidic patch of histone H2A/H2B. We further find that the more broadly conserved CENP-C motif uses the same mechanism for CENP-A nucleosome recognition. Our findings reveal a conserved mechanism for protein recruitment to centromeres and a histone recognition mode whereby a disordered peptide binds the histone tail through nucleosome-docking-facilitated hydrophobic interactions.

Our findings demonstrate the importance of hypertrophy and the unconventional cell division cycle of hepatocytes in regeneration, prompting a significant revision of the generally accepted model of liver regeneration.

The authors note that, due to a printer's error, references 41-50 appeared incorrectly. The corrected references follow. The authors note: "Our paper unfortunately missed reference to an earlier suggestion of the T6 structure (43). This work entitled 'A hypothetical dense 3,4-connected carbon net and related B 2 C and CN 2 nets built from 1,4-cyclohexadienoid units' by M. J. Bucknum and R. Hoffmann was published in J Am Chem Soc 116: 11456-11464 (1994), where the electronic structure of a hypothetical 3,4-connected tetragonal allotrope of carbon is discussed. The results in this article are consistent with what we find. The same group had also suggested a metallic carbon structure (44) that was published in J Am Chem Soc 105: 4831-4832 (1983), which we also missed to cite. We thank Prof. Hoffmann for bringing these papers to our attention."The complete references appear below. www.pnas.org/cgi