A probabilistic model of nuclear import of proteins
نویسندگان
چکیده
MOTIVATION Nucleo-cytoplasmic trafficking of proteins is a core regulatory process that sustains the integrity of the nuclear space of eukaryotic cells via an interplay between numerous factors. Despite progress on experimentally characterizing a number of nuclear localization signals, their presence alone remains an unreliable indicator of actual translocation. RESULTS This article introduces a probabilistic model that explicitly recognizes a variety of nuclear localization signals, and integrates relevant amino acid sequence and interaction data for any candidate nuclear protein. In particular, we develop and incorporate scoring functions based on distinct classes of classical nuclear localization signals. Our empirical results show that the model accurately predicts whether a protein is imported into the nucleus, surpassing the classification accuracy of similar predictors when evaluated on the mouse and yeast proteomes (area under the receiver operator characteristic curve of 0.84 and 0.80, respectively). The model also predicts the sequence position of a nuclear localization signal and whether it interacts with importin-α. AVAILABILITY http://pprowler.itee.uq.edu.au/NucImport
منابع مشابه
Promotion of importin α–mediated nuclear import by the phosphorylation-dependent binding of cargo protein to 14-3-3
14-3-3 proteins are phosphoserine/threonine-binding proteins that play important roles in many regulatory processes, including intracellular protein targeting. 14-3-3 proteins can anchor target proteins in the cytoplasm and in the nucleus or can mediate their nuclear export. So far, no role for 14-3-3 in mediating nuclear import has been described. There is also mounting evidence that nuclear i...
متن کاملThe Ty1 integrase protein can exploit the classical nuclear protein import machinery for entry into the nucleus
Like its retroviral relatives, the long terminal repeat retrotransposon Ty1 in the yeast Saccharomyces cerevisiae must traverse a permanently intact nuclear membrane for successful transposition and replication. For retrotransposition to occur, at least a subset of Ty1 proteins, including the Ty1 integrase, must enter the nucleus. Nuclear localization of integrase is dependent upon a C-terminal...
متن کاملMyosin‐1C uses a novel phosphoinositide‐dependent pathway for nuclear localization
Accurate control of macromolecule transport between nucleus and cytoplasm underlines several essential biological processes, including gene expression. According to the canonical model, nuclear import of soluble proteins is based on nuclear localization signals and transport factors. We challenge this view by showing that nuclear localization of the actin-dependent motor protein Myosin-1C (Myo1...
متن کاملA cytoplasmically anchored nuclear protein interferes specifically with the import of nuclear proteins but not U1 snRNA
A cytoplasmically anchored mutant SV40 T antigen, FS T antigen, was shown previously to interfere specifically with the nuclear import of a heterologous nuclear protein, adenovirus 5 fiber protein, in cultured monkey cells (Schneider, J., C. Schindewolf, K. van Zee, and E. Fanning. 1988. Cell. 54:117-125; van Zee, K., F. Appel, and E. Fanning. 1991. Mol. Cell. Biol. 11:5137-5146). In this repor...
متن کاملImport of plasmid DNA into the nucleus is sequence specific.
Nuclear import of plasmid DNA in nondividing cells is a process essential to the success of numerous viral life cycles, gene therapy protocols, and gene expression experiments. Here, intact protein-free SV40 DNA was cytoplasmically injected into cells and its subcellular localization was followed by in situ hybridization. SV40 DNA localized to the nucleus consistent with a mechanism of transpor...
متن کاملذخیره در منابع من
با ذخیره ی این منبع در منابع من، دسترسی به آن را برای استفاده های بعدی آسان تر کنید
برای دانلود متن کامل این مقاله و بیش از 32 میلیون مقاله دیگر ابتدا ثبت نام کنید
ثبت ناماگر عضو سایت هستید لطفا وارد حساب کاربری خود شوید
ورودعنوان ژورنال:
- Bioinformatics
دوره 27 9 شماره
صفحات -
تاریخ انتشار 2011