The alteration of DNA or protein in chromatin by the covalent addition or removal of chemical groups.

Any base modification or substitution events that result in alterations in the coding potential or structural properties of RNAs as a result of changes in the base-pairing properties of the modified ribonucleoside(s).

The conversion of a cytosine residue to uridine in an RNA molecule by deamination.

The enzymatic modification of the chemical structure of specific sites in mRNA.

The assembly and arrangement of the membrane of a peroxisome.

The import of proteins into the peroxisomal matrix. A peroxisome targeting signal (PTS) binds to a soluble receptor protein in the cytosol, and the resulting complex then binds to a receptor protein in the peroxisome membrane and is imported.

The division of a mature peroxisome within a cell to form two or more separate peroxisome compartments.

The regulated release of renin into the blood stream by juxtoglomerular cells.

regulation of angiotensin levels in blood

The process that modulates the level of angiotensin in the blood by balancing the maturation of renin substrate to mature angiotensin and the catabolism of mature angiotensin.

The process leading to the attainment of the full functional capacity of angiotensin by conversion of renin substrate into mature angiotensin in the blood.

A multiprotein complex that functions broadly in eukaryotic organisms as a transcriptional repressor of protein-coding genes, through the gene-specific deacetylation of histones. Amongst its subunits, the Sin3 complex contains Sin3-like proteins, and a number of core proteins that are shared with the NuRD complex (including histone deacetylases and histone binding proteins). The Sin3 complex does not directly bind DNA itself, but is targeted to specific genes through protein-protein interactions with DNA-binding proteins.

nucleosome remodeling and histone deacetylation complex

An approximately 2 MDa multi-subunit complex that exhibits ATP-dependent chromatin remodeling activity in addition to histone deacetylase (HDAC) activity, and has been shown to establish transcriptional repression of a number of target genes in both vertebrates and invertebrates. Amongst its subunits, the NuRD complex contains histone deacetylases, histone binding proteins and Mi-2-like proteins.