Accepted Article On the interaction of ribosomal protein RPL22e with microtubules Elena M. Chudinova 1,2 , Ilya B. Brodsky 3 , Elena S. Nadezhdina 1,3 1 Institute of Protein Research of Russian Academy of Science; Russia, 142290, Pushchino, Moscow Region, Institutskaya str., 4 2 Peoples' Friendship University of Russia (RUDN University); Russia 117198, Moscow, Miklukho-Maklaya str., 6 3 M.V. Lomonosov Moscow State University, Russia, 119991, Moscow, Leninskie Gory, 1-73 Running title: The interaction of RPL22e with microtubules Corresponding author: Elena M. Chudinova, chudiel@mail.ru Key words: TIRF microscopy, co-sedimentation, single molecule imaging, one- dimensional diffusion, p150 Glued List of abbreviations: MT microtubule TIRF total internal reflection fluorescence Abstract Microtubule (MT) protein preparations often contain components of the translation machinery, including ribosome proteins. To understand the biological meaning of it we studied the interaction of ribosomal protein RPL22e with the MT. We found that bacteria- expressed purified RPL22e-GFP-6His did co-sediment with brain tubulin MTs with 1.3 μM dissociation coefficient. Such a K D is comparable to some specific MT-associated proteins. Distinct in vitro interaction of RPL22e-GFP with MTs was also observed by TIRF microscopy. In real-time assay, RPL22e-GFP molecules stayed bound to MTs for several This article has been accepted for publication and undergone full peer review but has not been through the copyediting, typesetting, pagination and proofreading process, which may lead to differences between this version and the Version of Record. Please cite this article as doi: 10.1002/cbin.11141. This article is protected by copyright. All rights reserved. Elena Nadezhdina ORCID iD: 0000-0002-2899-6140