Proteins are the most abundant and diverse class of biomolecules that mediate the vast majority of biochemical processes. The functional units within a protein are the ”domains” which fold autonomously from the rest of the linear amino acid sequence in the protein. Novelty in protein function often arises as a result of gain, loss or re-shuffling of existing domains. Thus, protein domains can a...

PCV173 Are SPAniSh regionS imPlementing the nAtionAl therAPeutiC PoSitioning rePort (tPr) regArding new orAl AntiCoAgulAntS (noAC) in the SAme wAy? A CASe of regionAl VAriAbility in drug ACCeSS Rodriguez Barrios JM1, Pérez-Alcántara F2, Gonzalez-Juantey JR3, Avendaño C4, Suarez C5, López-Bastida J6, Barja de Soroa P1 1Daiichi-Sankyo, Madrid, Spain, 2OBLIKUE Consulting, Barcelona, Spain, 3Santia...

A major question in nuclear import concerns the identity of the nucleoporin(s) that interact with the nuclear localization sequences (NLS) receptor and its cargo as they traverse the nuclear pore. Ligand blotting and solution binding studies of isolated proteins have attempted to gain clues to the identities of these nucleoporins, but the studies have from necessity probed binding events far fr...

Regulated spindle orientation maintains epithelial tissue integrity and stem cell asymmetric cell division. In Drosophila melanogaster neural stem cells (neuroblasts), the scaffolding protein Canoe (Afadin/Af-6 in mammals) regulates spindle orientation, but its protein interaction partners and mechanism of action are unknown. In this paper, we use our recently developed induced cell polarity sy...

S100 proteins are a subfamily of the EF-hand type calcium sensing proteins, the exact biological functions of which have not been clarified yet. In this work, we have identified Cyclophilin 40 (CyP40) and FKBP52 (called immunophilins) as novel targets of S100 proteins. These immunophilins contain a tetratricopeptide repeat (TPR) domain for Hsp90 binding. Using glutathione-S transferase pull-dow...

Mitochondrial fission controls mitochondrial shape and physiology, including mitochondrial remodeling in apoptosis. During assembly of the yeast mitochondrial fission complex, the outer membrane protein Fis1 recruits the dynamin-related GTPase Dnm1 to mitochondria. Fis1 contains a tetratricopeptide repeat (TPR) domain and interacts with Dnm1 via the molecular adaptors Mdv1 and Caf4. By using cr...

Peroxins are proteins required for peroxisome assembly and are encoded by the PEX genes. The Yarrowia lipolytica pex5-1 mutant fails to import a subset of peroxisomal matrix proteins, including those with a type 1 peroxisomal targeting signal (PTS1). Pex5p family members interact with a PTS1 through their characteristic tetratricopeptide repeat (TPR) domain. We used binding assays in vitro to i...

We have two objectives. First, we want to build a system for detecting tetratricopeptide repeats in protein sequences. Second, we want to demonstrate how the general bioinformatics database integration system called Kleisli can help build such a system easily. We achieve these two objectives by showing that short and clear programs can be written in Kleisli, using its high-level query language ...

A putative spindle matrix has been hypothesized to mediate chromosome motion, but its existence and functionality remain controversial. In this report, we show that Megator (Mtor), the Drosophila melanogaster counterpart of the human nuclear pore complex protein translocated promoter region (Tpr), and the spindle assembly checkpoint (SAC) protein Mad2 form a conserved complex that localizes to ...