title: Systematically ranking the tightness of membrane association for peripheral membrane proteins (PMPs).
abstract: Large-scale quantitative evaluation of the tightness of membrane association for nontransmembrane proteins is important for identifying true peripheral membrane proteins with functional significance. Herein, we simultaneously ranked more than 1000 proteins of the photosynthetic model organism Synechocystis sp. PCC 6803 for their relative tightness of membrane association using a proteomic approach. Using multiple precisely ranked and experimentally verified peripheral subunits of photosynthetic protein complexes as the landmarks, we found that proteins involved in two-component signal transduction systems and transporters are overall tightly associated with the membranes, whereas the associations of ribosomal proteins are much weaker. Moreover, we found that hypothetical proteins containing the same domains generally have similar tightness. This work provided a global view of the structural organization of the membrane proteome with respect to divergent functions, and built the foundation for future investigation of the dynamic membrane proteome reorganization in response to different environmental or internal stimuli.
authors.affiliation: From the ‡State Key Laboratory of Molecular Developmental Biology, Institute of Genetics and Developmental Biology, Chinese Academy of Sciences, No.1 West Beichen Rd., Beijing 100101, China;
authors.forename: Liyan
authors.initials: L
authors.lastname: Gao
authors.affiliation: §State Key Laboratory of Microbial Technology, Shandong University, Jinan 250100, China;
authors.forename: Haitao
authors.initials: H
authors.lastname: Ge
authors.affiliation: From the ‡State Key Laboratory of Molecular Developmental Biology, Institute of Genetics and Developmental Biology, Chinese Academy of Sciences, No.1 West Beichen Rd., Beijing 100101, China;
authors.forename: Xiahe
authors.initials: X
authors.lastname: Huang
authors.affiliation: From the ‡State Key Laboratory of Molecular Developmental Biology, Institute of Genetics and Developmental Biology, Chinese Academy of Sciences, No.1 West Beichen Rd., Beijing 100101, China;
authors.forename: Kehui
authors.initials: K
authors.lastname: Liu
authors.affiliation: From the ‡State Key Laboratory of Molecular Developmental Biology, Institute of Genetics and Developmental Biology, Chinese Academy of Sciences, No.1 West Beichen Rd., Beijing 100101, China;
authors.forename: Yuanya
authors.initials: Y
authors.lastname: Zhang
authors.affiliation: ¶Department of Chemistry, University of Louisiana at Lafayette, Lafayette, Louisiana 70504.
authors.forename: Wu
authors.initials: W
authors.lastname: Xu
authors.affiliation: From the ‡State Key Laboratory of Molecular Developmental Biology, Institute of Genetics and Developmental Biology, Chinese Academy of Sciences, No.1 West Beichen Rd., Beijing 100101, China; ycwang@genetics.ac.cn.
authors.forename: Yingchun
authors.initials: Y
authors.lastname: Wang
mesh_terms: D001426:Bacterial Proteins / Q000737:chemistry / Q000378:metabolism*; D002462:Cell Membrane / Q000378:metabolism*; D008565:Membrane Proteins / Q000737:chemistry / Q000378:metabolism*; D011485:Protein Binding; D017434:Protein Structure, Tertiary; D020543:Proteome / Q000737:chemistry / Q000378:metabolism; D046939:Synechocystis / Q000378:metabolism*
chemical_list: D001426:Bacterial Proteins; D008565:Membrane Proteins; D020543:Proteome