Mass spectrometry reveals the chemistry of formaldehyde cross-linking in structured proteins

Tamar Tayri-Wilk; Moriya Slavin; Joanna Zamel; Ayelet Blass; Shon Cohen; Alex Motzik; Xue Sun; Deborah E. Shalev; Oren Ram; Nir Kalisman

doi:10.1038/s41467-020-16935-w

Nature Communications (Jun 2020)

Mass spectrometry reveals the chemistry of formaldehyde cross-linking in structured proteins

Tamar Tayri-Wilk,
Moriya Slavin,
Joanna Zamel,
Ayelet Blass,
Shon Cohen,
Alex Motzik,
Xue Sun,
Deborah E. Shalev,
Oren Ram,
Nir Kalisman

Affiliations

Tamar Tayri-Wilk: Institute of Life Sciences, The Hebrew University of Jerusalem
Moriya Slavin: Institute of Life Sciences, The Hebrew University of Jerusalem
Joanna Zamel: Institute of Life Sciences, The Hebrew University of Jerusalem
Ayelet Blass: Institute of Life Sciences, The Hebrew University of Jerusalem
Shon Cohen: Institute of Life Sciences, The Hebrew University of Jerusalem
Alex Motzik: Institute of Life Sciences, The Hebrew University of Jerusalem
Xue Sun: Institute of Life Sciences, The Hebrew University of Jerusalem
Deborah E. Shalev: Wolfson Centre for Applied Structural Biology, The Hebrew University of Jerusalem
Oren Ram: Institute of Life Sciences, The Hebrew University of Jerusalem
Nir Kalisman: Institute of Life Sciences, The Hebrew University of Jerusalem

DOI: https://doi.org/10.1038/s41467-020-16935-w
Journal volume & issue: Vol. 11, no. 1
pp. 1 – 9

Abstract

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Formaldehyde (FA) is a popular cross-linking reagent, but applying it for cross-linking mass spectrometry (XLMS) has been largely unsuccessful. Here, the authors show that cross-links in structured proteins are the product of two FA molecules and identify hundreds of FA cross-links by XLMS in vitro and in situ.

Published in Nature Communications

ISSN: 2041-1723 (Online)
Publisher: Nature Portfolio
Country of publisher: United Kingdom
LCC subjects: Science
Website: https://www.nature.com/ncomms/

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