Complex domain formation

The centromere–kinetochore complex is a highly specialized chromatin domain that both mediates and monitors chromosome–spindle interactions responsible for accurate partitioning of sister chromatids to daughter cells. Centromeres are distinguished from adjacent chromatin by specific patterns of histone modification and the presence of a centromere-specific histone H3 variant (e.g. CENP-A). Centromere-proximal regions usually correspond to sites of avid and persistent sister chromatid cohesion mediated by the conserved cohesin complex.

15p research12 01-06-2013 49 4   Download

Tripeptidyl-peptidase II (TPP II) is a large (Mr106 ) tripeptide-releasing enzyme with an active site of the subtil-isin-type. Compared with other subtilases, TPP II has a 200 amino-acid insertion between the catalytic Asp44 and His264 residues, and is active as anoligomeric complex. This study demonstrates that the insert is important for the formation of the active high-molecular mass complex.

6p research12 29-04-2013 37 3   Download

The three-dimensional crystal structure of recombinant annexin Gh1 fromGossypium hirsutum(cotton fibre) has been determined and refined to the finalR-factor of 0.219 at the resolution of 2.1 A ˚ . This plant annexin consists of the typical
annexin fold and is similar to the previously solved bell pepper annexinAnx24(Ca32), but significant differences are seen when compared to the structure of nonplant annexins.

8p fptmusic 16-04-2013 39 2   Download

The oxaloacetate decarboxylase Na + pumps OAD-1 and OAD-2 ofVibrio choleraeare composed of a peripherala-subunit associated with two integ-ral membrane-bound subunits (bandc). The a-subunit contains the carb-oxyltransferase domain in its N-terminal portion and the biotin-binding domain in its C-terminal portion. Thec-subunit plays a profound role in the assembly of the complex.

10p awards 05-04-2013 34 4   Download

In eukaryotes, CpG methylation is an epigenetic DNA modification that is important for heterochromatin formation. Centromere protein B (CENP-B) specifically binds to the centromeric 17 base-pair CENP-B box DNA, which contains two CpG dinucleotides. In this study, we tested complex formation by the DNA-binding domain of CENP-B with methylated and unmethylated CENP-B box DNAs, and found that CENP-B preferentially binds to the unmethylated CENP-B box DNA.

8p awards 05-04-2013 30 5   Download

Subunitbis indispensable for the formation of a functional H + -translocating FOcomplex both in vivo andin vitro. Whereas the very C-terminus of subunitbinteracts with F1 and plays a crucial role in enzyme assembly, the C-terminal region is also considered to be necessary for proper recon-stitution of FOinto liposomes. Here, we show that a syn-thetic peptide, residues 1–34 of subunitb(b1)34 ) [Dmitriev, O., Jones, P.C., Jiang,W. & Fillingame, R.H. (1999)J. Biol. Chem.

7p awards 05-04-2013 46 3   Download

Repression of poly(A)-binding protein (PABP) mRNA translation involves the formation of a heterotrimeric ribonucleoprotein complex by the binding of PABP, insulin-like growth factor II mRNA binding protein-1 (IMP1) and theunrgene encoded polypeptide (UNR) to the adenine-rich autoregu-latory sequence (ARS) located at the 5¢ untranslated region of the PABP-mRNA.

13p inspiron33 23-03-2013 32 3   Download