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a Related Biological Terms:

cross-reacting material

A protein product resulting from mutation that has lost its function but is recognizable by its ability to react with antibodies raised against the normal protein. More broadly, material may cross-react because it bears an epitope in common with the antigen.

cross-regulation

control of a metabolic pathway by the product of a different but related pathway, e.g. activation of the reduction of ADP to dADP by dGTP.

cross-species chromosome painting

(see zoo-fluorescence in situ hybridization)

cubane

see iron-sulphur protein

cyclic amplification and selection of targets (CASTing)

Essentially identical to the selected and amplified (protein) binding site oligonucleotide (SAAB) and target detection assay (TDA) procedures; a procedure for identification of consensus sequences of DNA to which a protein, e.g. a transcription factor, may bind. A random polynucleotide sequence is synthesized flanked by two defined sequences that will serve as templates for PCR primers; the polynucleotides are exposed to the DNA-binding protein, any complex that is formed is separated from the unliganded polynucleotides (e.g. by gel shift assay, affinity chromatography, filter binding) and the polynucleotide of the complex is isolated and amplified by PCR; repeated recycling through the sequence of ligand formation, selection and amplification results in a preparation that is sufficiently pure to be cloned into bacteria for larger-scale production. A variant is systematic evolution of ligands by exponential enrichment (SELEX) for identification of RNA sequences, which begins with a mixture of polyribonucleotides and in each cycle produces DNA from the selected RNA-protein complex using reverse transcriptase, amplifies it by PCR, and then produces new RNA transcripts for the next round of selection. CASTing: Wright, W.E. and Funk, W.D. (1993) Trends Biochem. Sci. 18, 77-80; SAAB: Blackwell, T.K. and Weintraub, H.W. (1990) Science 250, 1104-1110; SELEX: Turek, C. and Gold, L. (1990) Science 249, 505-510; TDA: Thiesen, H.-J. and Bach, C. (1990) Nucleic Acids Res. 18, 3203-3209; Ouellette, M.M. and Wright, W.E. (1995) Curr. Opin. Biotechnol. 6, 65-72 Recommended reading: lipofectamine 2000 protocol

cystatin

A term applied both to the superfamily of cysteine proteinase inhibitors and to one subgroup; the other subgroups are the kininogens and stefins.

cysteine proteinase (thiol proteinase)

A type of peptidase that has at its active site a cysteine residue. (see also aspartate proteinase; metalloproteinase; serine proteinase)

cysteine proteinase inhibitor

(see alpha1 α1)-cysteine proteinase inhibitor; kininogen)

cysteine scanning

The use of site-directed mutagenesis to determine, for residues of a complex, usually an uncrystallized protein, their proximity to other residues of the protein, their mileiu (extracellular, cytoplasmic, transmembrane) or the participation of the residues' side chains in specific interactions. Every residue of a protein is systematically replaced by a cysteine residue. Being of a moderate size so that physical disruption is unlikely to cause changes in function, and being easily converted into a useful reporter group by chemical modification, cysteine is a generally useful residue for modification.Frillingos, S., Sahin-Toth. M., Wu, J. and Kaback, H.R. (1998) FASEB J. 12, 1281-1299 Related tool: molecular biology tools

cytoplasm

The part of a cell inside the plasma membrane and outside the nucleus, comprising membrane-bound organelles, cytoskeleton, ribosomes and cytosol.

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