Journal Article

PUBDB-2024-06660

http://join2-wiki.gsi.de/foswiki/pub/Main/Artwork/join2_logo100x88.png Crystal structures of cables formed by the acetylated and unacetylated forms of the Schizosaccharomyces pombe tropomyosin orthologue TpmCdc8

Reinke, P. Y. A.CFEL*DESY* ; Heiringhoff, R. S.Extern*EMBL* ; Reindl, T. ; Baker, K. ; Taft, M. H.Extern*XFEL.EU* ; Meents, A.CFEL*XFEL.EU*DESY* ; Mulvihill, D. P. ; Davies, O. R. ; Fedorov, R.Extern* ; Zahn, M.Extern*EMBL* ; Manstein, D. J. (Corresponding author)Extern*CSSB*

2024
American Soc. for Biochemistry and Molecular Biology Bethesda, MD

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Please use a persistent id in citations: doi:10.1016/j.jbc.2024.107925  doi:10.3204/PUBDB-2024-06660

Abstract: Cables formed by head-to-tail polymerization of tropomyosin, localized along the length of sarcomeric and cytoskeletal actin filaments, play a key role in regulating a wide range of motile and contractile processes. The stability of tropomyosin cables, their interaction with actin filaments and the functional properties of the resulting co-filaments are thought to be affected by N-terminal acetylation of tropomyosin. Here, we present high-resolution structures of cables formed by acetylated and unacetylated Schizosaccharomyces pombe tropomyosin orthologue TpmCdc8. The crystal structures represent different types of cables, each consisting of TpmCdc8 homodimers in a different conformation. The structures show how the interactions of the residues in the overlap junction contribute to cable formation and how local structural perturbations affect the conformational dynamics of the protein and its ability to transmit allosteric signals. In particular, N-terminal acetylation increases the helicity of the adjacent region, which leads to a local reduction in conformational dynamics and consequently to less fraying of the N-terminal region. This creates a more consistent complementary surface facilitating the formation of specific interactions across the overlap junction.

Note: ISSN 0021-9258 not unique: **2 hits**. erman Research Foundation (DFG), Grant FE1510/2-1, and the Cluster of Excellence RESIST (Resolving InfectionSusceptibility; EXC 2155), project ID: 39087428

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Contributing Institute(s):

1. FS-CFEL-1 Fachgruppe BMX (FS-CFEL-1-BMX)
2. CFEL-Coherent X-Ray Imaging (FS-CFEL-1)

Research Program(s):

1. 633 - Life Sciences – Building Blocks of Life: Structure and Function (POF4-633) (POF4-633)
2. 6G3 - PETRA III (DESY) (POF4-6G3) (POF4-6G3)
3. DFG project G:(GEPRIS)390874280 - EXC 2155: RESIST - Resolving Infection Susceptibility (390874280) (390874280)

Experiment(s):

1. PETRA Beamline P13 (PETRA III)

Appears in the scientific report 2024

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