A bimodal distribution of two distinct categories of intrinsically disordered structures with separate functions in FG nucleoporins.

Nuclear pore complexes (NPCs) gate the only conduits for nucleocytoplasmic transport in eukaryotes. Their gate is formed by nucleoporins containing large intrinsically disordered domains with multiple phenylalanine-glycine repeats (FG domains). In combination, these are hypothesized to form a structurally and chemically homogeneous network of random coils at the NPC center, which sorts macromolecules by size and hydrophobicity.

Characterization of the PL-I-related SP2 protein from Xenopus.

The complete cDNA sequence of Xenopus laevis sperm specific proteins SP1 and SP2 has been determined. This information when taken together with N-terminal sequencing and mass spectroscopy data indicates that these two proteins share a product precursor relationship in which SP2 results from cleavage of a short N-terminal peptide of SP1. The secondary and tertiary structures of SP2 have been characterized using circular dichroism and three dimension structure prediction.

Long-range histone acetylation: biological significance, structural implications, and mechanisms.

Genomic characterization of various euchromatic regions in higher eukaryotes has revealed that domain-wide hyperacetylation (over several kb) occurs at a range of loci, including individual genes, gene family clusters, compound clusters, and more general clusters of unrelated genes. Patterns of long-range histone hyperacetylation are strictly conserved within each unique cellular system studied and they reflect biological variability in gene regulation. Domain-wide histone acetylation consists generally of nonuniform peaks of enriched hyperacetylation of specific core histones, histone isoforms, and (or) histone variants against a backdrop of nonspecific acetylation across the domain in question.