2Gram Features Based Prediction of Membrane Protein Types Using Ensemble Classifiers Methods

2019 ◽

Vol 8 (12) ◽

pp. 3131-3137

Keyword(s):

Feature Extraction ◽

Amino Acid ◽

Membrane Protein ◽

Amino Acid Composition ◽

Acid Composition ◽

Extraction Method ◽

Ensemble Classifiers ◽

Pseudo Amino Acid Composition ◽

Adaptive Boosting ◽

Feature Extraction Method

Membrane protein are very important and play significantly in the field of biology and medicine. The main purpose is to find suitable features of a membrane protein. Various features extraction methods are use to find membrane protein and their types. PseAAC (Pseudo Amino Acid Composition) is a one of the feature extraction method which was used to find the localization of the protein, which helps in the detection of membrane types. Therefore, in this study, a novel feature extraction method which is an integration of the pseudo amino acid composition integer values mapped in discrete sequence numbers in a matrix. The proposed scheme avoids biasing among the different membrane proteins and their types. Decision making for predicting the identification of membrane protein types was performed using an algorithm framework to improve the learning accuracy, by putting the training samples weights in the learning process of AdaBoost. The performance of different ensemble classifiers such as Random Forest, AdaBoost, is analyzed. The best accuracy achieved is 91.50% for with the Matthews correlation coefficient is 83.0%, and Cohen’s Kappa value is 82.7%

Download Full-text

TMCC3 localizes at the three-way junctions for the proper tubular network of the endoplasmic reticulum

Biochemical Journal ◽

10.1042/bcj20190359 ◽

2019 ◽

Vol 476 (21) ◽

pp. 3241-3260

Author(s):

Sindhu Wisesa ◽

Yasunori Yamamoto ◽

Toshiaki Sakisaka

Keyword(s):

Endoplasmic Reticulum ◽

Membrane Proteins ◽

Membrane Protein ◽

Mammalian Cells ◽

Coiled Coil ◽

Transmembrane Domains ◽

Domain Family ◽

Coiled Coil Domain ◽

U2os Cells ◽

Er Membrane

The tubular network of the endoplasmic reticulum (ER) is formed by connecting ER tubules through three-way junctions. Two classes of the conserved ER membrane proteins, atlastins and lunapark, have been shown to reside at the three-way junctions so far and be involved in the generation and stabilization of the three-way junctions. In this study, we report TMCC3 (transmembrane and coiled-coil domain family 3), a member of the TEX28 family, as another ER membrane protein that resides at the three-way junctions in mammalian cells. When the TEX28 family members were transfected into U2OS cells, TMCC3 specifically localized at the three-way junctions in the peripheral ER. TMCC3 bound to atlastins through the C-terminal transmembrane domains. A TMCC3 mutant lacking the N-terminal coiled-coil domain abolished localization to the three-way junctions, suggesting that TMCC3 localized independently of binding to atlastins. TMCC3 knockdown caused a decrease in the number of three-way junctions and expansion of ER sheets, leading to a reduction of the tubular ER network in U2OS cells. The TMCC3 knockdown phenotype was partially rescued by the overexpression of atlastin-2, suggesting that TMCC3 knockdown would decrease the activity of atlastins. These results indicate that TMCC3 localizes at the three-way junctions for the proper tubular ER network.

Download Full-text