Native and tagged CENP-A histones are functionally inequivalent.

ABSTRACT:

Background

Over the past several decades, the use of biochemical and fluorescent tags has elucidated mechanistic and cytological processes that would otherwise be impossible. The challenging nature of certain nuclear proteins includes low abundancy, poor antibody recognition, and transient dynamics. One approach to get around those issues is the addition of a peptide or larger protein tag to the target protein to improve enrichment, purification, and visualization. However, many of these studies were done under the assumption that tagged proteins can fully recapitulate native protein function.

Results

We report that when C-terminally TAP-tagged CENP-A histone variant is introduced, it undergoes altered kinetochore protein binding, differs in post-translational modifications

SUBMITTER: Bui M 

PROVIDER: S-EPMC11145777 | biostudies-literature | 2024 Jun

REPOSITORIES: biostudies-literature