Taxonomic distribution of proteins containing CENPB domains

The tree below includes only several representative species and genera. The complete taxonomic breakdown of all proteins containing CENPB domains can be accessed here. Click the counts or percentage values to display the corresponding proteins.

Epileptic seizures caused by inactivation of a novel gene, jerky, relatedto centromere binding protein-B in transgenic mice.

Toth M, Grimsby J, Buzsaki G, Donovan GP
Nat Genet. 1995; 11: 71-5

Epidemiological data and genetic studies indicate that certain forms ofhuman epilepsy are inherited. Based on the similarity between the humanand mouse genomes, mouse models of epilepsy could facilitate the discoveryof genes associated with epilepsy syndromes. Here, we report aninsertional murine mutation that inactivates a novel gene and results inwhole body jerks, generalized clonic seizures, and epileptic brainactivity in transgenic mice. The gene, named jerky, encodes a putative41.7 kD protein displaying homology to a number of nuclear regulatoryproteins, suggesting that perhaps the jerky protein is able to bind DNA.

An ancient family of embryonically expressed mouse genes sharing a conserved protein motif with the T locus.

Bollag RJ, Siegfried Z, Cebra-Thomas JA, Garvey N, Davison EM, Silver LM
Nat Genet. 1994; 7: 383-9

The T locus encodes a product with DNA binding activity that is likely to play a role in the development of all vertebrate organisms. We have identified and characterized a novel family of mouse genes that share a protein motif, the T-box, with the prototypical T locus. The T-box domain of the T locus co-localizes with its DNA binding activity. Each T-box gene is expressed in a unique temporal and spatial pattern during embryogenesis. Phylogenetic analysis suggests that at least three T-box genes were present in the common ancestor to vertebrates and invertebrates. Thus, members of the T-box family could have played a role in the evolution of all metazoan organisms.

Homeodomain-DNA recognition.

Gehring WJ, Qian YQ, Billeter M, Furukubo-Tokunaga K, Schier AF, Resendez-Perez D, Affolter M, Otting G, Wuthrich K
Cell. 1994; 78: 211-23

A human centromere protein, CENP-B, has a DNA binding domain containingfour potential alpha helices at the NH2 terminus, which is separable fromdimerizing activity.

Yoda K, Kitagawa K, Masumoto H, Muro Y, Okazaki T
J Cell Biol. 1992; 119: 1413-27

The alphoid DNA-CENP-B (centromere protein B) complex is the firstsequence-specific DNA/protein complex detected in the centromeric regionof human chromosomes. In the reaction, CENP-B recognizes a 17-bp sequence(CENP-B box) and assembles two alphoid DNA molecules into a complex, whichis designated complex A (Muro, Y., H. Masumoto, K. Yoda, N. Nozaki, M.Ohashi, and T. Okazaki. 1992. J. Cell Biol. 116:585-596). Since CENP-Bgene is conserved in mammalian species and CENP-B boxes are found also inmouse centromere satellite DNA (minor satellite), this sequence-specificDNA-protein interaction may be important for some kind of commoncentromere function. In this study we have characterized the structure ofCENP-B and CENP-B-alphoid DNA complex. We have shown by chemicalcross-linking that CENP-B formed a dimer, and have estimated by molecularweight determination the composition of complex A to be a CENP-B dimer andtwo molecules of alphoid DNA. The DNA binding domain has been delimitedwithin the NH2-terminal 125-amino acid region containing four potentialalpha-helices using truncated CENP-B made in Escherichia coli cells. Wehave shown that CENP-B had sites highly sensitive to proteases and thatthe DNA binding domain was separable from the dimerizing activity by theproteolytic cleavage at 20 kD from the COOH terminus of the molecule.Thus, CENP-B may organize a higher order structure in the centromere byjuxtaposing two CENP-B boxes in the alphoid DNA repeat through both theDNA-protein and protein-protein interactions.

The TEA domain: a novel, highly conserved DNA-binding motif.

Burglin TR
Cell. 1991; 66: 11-2