the gpi anchor signal sequence dictates the folding and functionality of the als5 adhesin from candida albicansgpi锚信号序列的折叠和功能要求als5 adhesin白色念珠菌.pdfVIP

The GPI Anchor Signal Sequence Dictates the Folding and Functionality of the Als5 Adhesin from Candida albicans 1,2 1 3 4 1 2 Mohammad Faiz Ahmad , Bhawna Yadav , Pravin Kumar , Amrita Puri , Mohit Mazumder , Anwar Ali , 1 1 1 Samudrala Gourinath , Rohini Muthuswami , Sneha Sudha Komath * 1 School of Life Sciences, Jawaharlal Nehru University, New Delhi, India, 2 Department of Chemistry, Jamia Millia Islamia, New Delhi, India, 3 Department of Plant Molecular Biology, University of Delhi, New Delhi, India, 4 Invisible Sentinel, Biotech Company, Philadelphia, Pennsylvania, United States of America Abstract Background: Proteins destined to be Glycosylphosphatidylinositol (GPI) anchored are translocated into the ER lumen completely before the C-terminal GPI anchor attachment signal sequence (SS) is removed by the GPI-transamidase and replaced by a pre-formed GPI anchor precursor. Does the SS have a role in dictating the conformation and function of the protein as well? Methodology/Principal Findings: We generated two variants of the Als5 protein without and with the SS in order to address the above question. Using a combination of biochemical and biophysical techniques, we show that in the case of Als5, an adhesin of C. albicans, the C-terminal deletion of 20 amino acids (SS) results in a significant alteration in conformation and function of the mature protein. Conclusions/Significance: We propose that the locking of the conformation of the precursor protein in an alternate conformation from that of the mature protein i