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The protein Tom40 is the main component of the outer membrane translocation machinery for mitochondrial preproteins. A new study extends the understanding of the molecular function of Tom40, suggesting that the pore-forming protein may interact with unfolded preprotein segments to protect against aggregation.
In response to DNA double-strand breaks, histone H1.2 translocates from the nucleus into the cytoplasm, leading to the mitochondrial release of cytochrome c and subsequent apoptosis of the cell. The molecular underpinnings for these processes remain enigmatic.
Although zinc fingers are best known to interact with DNA, they can, as in the case of the TFIIIA protein, also interact with RNA. A recent crystal structure reveals that zinc fingers can take advantage of the variability of RNA structure to recognize a particular RNA fragment.
Recent studies suggest that the Spt16 protein of FACT shuttles H2A–H2B dimers off and on nucleosomes during transcription elongation. By restoring nucleosomes after passage of RNA polymerase II, Spt16 and Spt6 prevent transcription from cryptic promoters in coding regions that would otherwise be expressed in the absence of histones.
The new crystal structure of the IRF-3 transactivation domain reveals an evolutionarily conserved protein domain whose activity is modulated by phosphorylation controlling oligomerization and protein-protein interactions.
Two recent reports show that the rate of transcription elongation affects splice site selection and exon skipping and, thereby, the nature of the information expressed from a gene.
The Hindu goddess Maha Devi is represented as having the power both to make and to destroy. Reminiscent of such power, two recent studies highlight the roles that nucleases play in both making and destroying RNAs associated with the mysterious world of small RNAs.
What prevents the replisome complex from moving along the DNA or breaking down when the replication fork stalls or encounters a DNA lesion? A recent paper describes how checkpoint proteins, Mrc1 and Tof1 couple the replisome to DNA synthesis.
Four recent studies demonstrate that closing of a cleft in the myosin head is required for actin binding and nucleotide release. This represents a major breakthrough in understanding actomyosin-based motility.
Recent studies of a tRNA guanine transglycosylase—a modifying enzyme known in all kingdoms of life—show how an unexpected active site aspartate becomes covalently attached to the tRNA substrate during catalysis, and how subsequent base exchange occurs in a single active site.
How does the C-terminal domain (CTD) of RNA polymerase II interact specifically with multiple targets? A recent paper describing the structure of this domain with a mRNA capping enzyme guanylyltransferase suggests that the CTD is a contortionist that, upon post-translational modification, adopts different configurations specifically recognized by its partners.
A recent study demonstrates that, when searching for the smallest active ribozymes, researchers may have thrown away parts that are important for functions.
Recent ensemble and single molecule manipulation studies highlight the mechanical nature of protein unfolding in vivo and, thus, the greater need to understand the response of proteins to mechanical force.
Don't prejudge the function of a domain based on its sequence. Two recent studies drive home this message and add the sterile-α motif (SAM) to the growing list of domains that are able to interact with both proteins and nucleic acids.
