Sulfation, the up-and-coming post-translational modification: Its role and mechanism in protein-protein interaction

Amina S. Woods, Hay Yan J Wang, Shelley N. Jackson

Research output: Contribution to journalArticle

Abstract

Tyrosine sulfation is a post-translational modification entailing covalent attachment of sulfate to tyrosine residues. It takes place in the trans-Golgi, is necessary for the bioactivity of some proteins, and improves their ability to interact with other proteins. In the present work, we show that a protein containing a sulfated tyrosine with a delocalized negative charge forms a salt bridge with another protein if it has two or more adjacent arginine residues containing positive delocalized charges. These noncovalent complexes are so stable that, when submitted to collision induced dissociation, the peptides forming the complex dissociate. Just one covalent bond fragments, the covalent bond between the tyrosine oxygen and the SO3 sulfur, and is represented by the appearance of a new peak (basic peptide + SO3), suggesting that in some instances covalent bonds will break down before the noncovalent bonds between the arginine guanidinium and SO3 dissociate. The data implies that the dissociation pathway is preferred; however, fragmentation between tyrosine and the sulfate residue is a major pathway.

Original languageEnglish (US)
Pages (from-to)1176-1182
Number of pages7
JournalJournal of Proteome Research
Volume6
Issue number3
DOIs
StatePublished - Mar 2007
Externally publishedYes

Keywords

  • Guanidium group
  • Noncovalent interactions
  • Salt bridges
  • Sulfation

ASJC Scopus subject areas

  • Genetics
  • Biotechnology
  • Biochemistry

Fingerprint Dive into the research topics of 'Sulfation, the up-and-coming post-translational modification: Its role and mechanism in protein-protein interaction'. Together they form a unique fingerprint.

  • Cite this