An organelle found in bacteria consisting of a proteinaceous coat containing enzymes for the degradation of 1,2-propanediol whose purpose is the protection of the rest of the cell from the toxic propionaldehyde product of the enzyme diol dehydratase.

Binding to a class III myosin; myosin III is monomeric and has an N terminal kinase domain.

A myosin complex containing one or more class IV myosin heavy chains and associated light chains; myosin IV is relatively uncharacterized, but is predicted to have a single motor domain, one IQ motif and a tail with a Myosin Tail Homology (myTH4) domain homologous to that in the tails of myosins VII and XV.

A myosin complex containing a dimer of class V myosin heavy chains and associated light chains; involved in intracellular transport. Myosin V is a dimeric molecule consisting of conserved motor domains followed by 6 IQ motifs which bind specific light chains and calmodulin. The tail domain is important for cellular localization and cargo binding and can be divided into an alpha-helical coiled coil region and a C-terminal globular region.

A myosin complex containing one or more class VI myosin heavy chains and associated light chains. Myosin VI has a single IQ motif in the neck and a tail region with a coiled coil domain followed by a unique globular domain; a unique insertion that enables myosin VI to move towards the pointed or minus end of actin filaments.

A myosin complex containing a dimer of class VII myosin heavy chains and associated light chains. Myosin VII (240 kDa) is predicted to be a dimeric molecule with 5 IQ motifs and a tail region with a short stretch of coiled coil followed by two myosin-tail homology (MyTH4) domains, two talin-binding (FERM) domains and an SH3-domain.

A myosin complex containing a dimer of class VIII myosin heavy chains and associated light chains. Myosin VIII is predicted to be dimeric, and contain an unusual 100-190 residue N-terminal extension prior to their motor domains, 3-4 IQ motifs, a short region (~70 residues) of predicted alpha-helical coiled coil and a C-terminal domain.

A myosin complex containing a class IX myosin heavy chain and associated light chains. Myosin IX is monomeric with a motor domain containing an N-terminal extension and an insert in the actin binding interface, followed by four to six IQ motifs and a tail region that contains a zinc binding motif and a domain with homology to GTPase activating proteins (GAPs) of the Rho family of G-proteins.

Binding to the DNA portion of a nucleosome.

Binding to DNA that is assembled into chromatin.

OBSOLETE. Binding to a histone that is assembled into a nucleosome.

Any process that modulates the frequency, rate or extent of mating type switching, the conversion of a single-cell organism from one mating type to another by the precise replacement of a DNA sequence at the expressed mating type locus with a copy of a sequence from a donor locus.

Any process that stops, prevents, or reduces the frequency, rate or extent of mating type switching.

Any process that activates or increases the frequency, rate or extent of mating type switching.

OBSOLETE. The controlled breakdown of chromatin from a higher order structure into its simpler subcomponents, DNA, histones, other proteins, and sometimes RNA.

A multiprotein complex having distributive polyadenylation activity of a variety of RNA substrates including hypomodified and incorrectly folded tRNAs, pre-snRNAs, pre-snoRNAs, incorrectly spliced or processed pre-mRNAs, cryptic unstable transcripts (CUTs), pre-rRNAs and rRNA fragments released as part of rRNA processing. In S. cerevisiae, the complex consists of either Pap2 (also known as Trf4) or Trf5, Air1 or Air2, and Mtr4, and is involved in RNA 3'-end processing and in RNA surveillance and quality control.

The process in which a pre-tRNA molecule is converted to a mature tRNA, ready for addition of an aminoacyl group.

The import of RNA from the cytoplasm to the nucleus.

The directed movement of mRNA from the nucleus to the cytoplasm.