A direct interaction between CPF and RNA Pol II links RNA 3' end processing to transcription.

Transcription termination by RNA polymerase II (RNA Pol II) is linked to RNA 3' end processing by the cleavage and polyadenylation factor (CPF or CPSF). CPF contains endonuclease, poly(A) polymerase, and protein phosphatase activities, which cleave and polyadenylate pre-mRNAs and dephosphorylate RNA Pol II to control transcription. Exactly how the RNA 3' end processing machinery is coupled to transcription remains unclear.

Role of Optimal Features Selection with Machine Learning Algorithms for Chest X-ray Image Analysis.

Introduction: The objective of the present study is to classify chest X-ray (CXR) images into COVID-positive and normal categories with the optimal number of features extracted from the images. The successful optimal feature selection algorithm that can represent images and the classification algorithm with good classification ability has been determined as the result of experiments.

Materials And Methods: This study presented a framework for the automatic detection of COVID-19 from the CXR images.

Deep Learning Approach for Analyzing the COVID-19 Chest X-Rays.

Purpose: The purpose of this study is to analyze the utility of Convolutional Neural Network (CNN) in medical image analysis. In this study, deep learning (DL) models were used to classify the X-ray into COVID, viral pneumonia, and normal categories.

Materials And Methods: In this study, we have compared the results 9 layers CNN model (9 LC) developed by us with 2 transfer learning models (Visual Geometry Group) 16 and VGG19.

Three-layered control of mRNA poly(A) tail synthesis in .

Biogenesis of most eukaryotic mRNAs involves the addition of an untemplated polyadenosine (pA) tail by the cleavage and polyadenylation machinery. The pA tail, and its exact length, impacts mRNA stability, nuclear export, and translation. To define how polyadenylation is controlled in , we have used an in vivo assay capable of assessing nuclear pA tail synthesis, analyzed tail length distributions by direct RNA sequencing, and reconstituted polyadenylation reactions with purified components.

Structural basis for inhibition of an archaeal CRISPR-Cas type I-D large subunit by an anti-CRISPR protein.

A hallmark of type I CRISPR-Cas systems is the presence of Cas3, which contains both the nuclease and helicase activities required for DNA cleavage during interference. In subtype I-D systems, however, the histidine-aspartate (HD) nuclease domain is encoded as part of a Cas10-like large effector complex subunit and the helicase activity in a separate Cas3' subunit, but the functional and mechanistic consequences of this organisation are not currently understood. Here we show that the Sulfolobus islandicus type I-D Cas10d large subunit exhibits an unusual domain architecture consisting of a Cas3-like HD nuclease domain fused to a degenerate polymerase fold and a C-terminal domain structurally similar to Cas11.