A mitochondria-localized glutamic acid-rich protein (MGARP/OSAP) is highly expressed in retina that exhibits a large area of intrinsic disorder |
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Authors: | Shaoling Qi Yifeng Wang Mingxue Zhou Yunxiao Ge Yongbin Yan Jian Wang Samuel Shao-Min Zhang Shuping Zhang |
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Institution: | (1) Department of Biological Sciences and Biotechnology, State-Key Lab of Biomembranes and Membrane Biotechnology, Tsinghua University, Haidian District, 100084 Beijing, China;(2) Department of Pathology, Yale University School of Medicine, 310 Cedar Street, BML 117, New Haven, CT 06520-8023, USA;(3) Present address: Pennsylvania State Hershey Medical Center, 500 University Drive, Hershey, PA 17033, USA; |
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Abstract: | Study of retina specific genes would offer insights into retinal diseases and treatment. Based on the information from the
gene expression profiles of mouse retinas, we here identified a mitochondria-localized glutamic acid-rich protein (MGARP/OSAP) as one of the highly expressed proteins in retina. Sequence analysis revealed that mouse and rat MGARPs
have an extra insertion of four consecutive amino acid repeats at the C-terminus, while other homologues do not. MGARP was
demonstrated to be localized to the mitochondria and overexpression of MGARP missing N-terminal region causes severe mitochondrial
aggregation, implying an important role of MGARP in maintaining mitochondrial morphology. MGARP is highly expressed in mitochondria-rich
layers, including inner segment of the photoreceptor, outer plexiform layer and ganglion cell layers of mouse retina. Far-UV
CD spectrum analysis suggested that MGARP exhibits a large area of intrinsic disorder and the unusual position of its Tyr
fluorescence suggested that Tyr residues in MGARP might form excimer and exist in an ionized state. These findings implied
that MGARP be a good candidate for assembling certain ion channels on mitochondria membrane and have great potential to be
involved in retinal energetic metabolism through mitochondria related pathway. |
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