PLK-1 regulates multiple steps during oocyte meiosis I and is recruited to meiotic chromosomes through a dual mechanism involving BUB-1 and CENP-C.

A comprehensive structural, biochemical, and cell biological analysis reveals the molecular mechanism and significance of the conserved interaction of centromeric protein N (CENP-N) with the centromeric nucleosome.

Centromeric protein M (CENP-M) is required for the stabilization of a quaternary complex that plays a crucial role in kinetochore organization and function.

The centromeric protein CENP-T assembles the microtubule-binding interface of kinetochores through direct recruitment of two Ndc80 complexes and indirect recruitment of a third one through the Mis12 complex.

A novel analytical workflow to quantitatively track motions of thousands of nucleosomes within chromatin fibers by high-speed atomic force microscopy.

The chromosomal passenger complex interacts with the inner kinetochore COMA complex through the Ctf19 C-terminus in vitro which is shown to be important for mediating accurate chromosome segregation.

Worm holocentromeres show a polycentric distribution, with each site containing a single centromeric nucleosome and also being targeted by multiple transcription factors.

The outer domain of the kinetochore can rotate (swivel) around the centromere, and this rather than intra-kinetochore stretching is coupled to anaphase onset.

Centromere deletion in Cryptococcus deuterogattii results in neocentromeres, which span actively expressed genes and at elevated temperatures cen10∆ mutants are unstable leading to chromosome fusion and silencing of the neocentromere.

Linker histone H1.8 shapes mitotic chromosomes by tuning the number and size of condensin-dependent DNA loops and suppressing condensin and DNA topoisomerase II-dependent individualization.