Conformational stability of six truncated cHMG1a proteins studied in their mixture by H/D exchange and electrospray ionization mass spectrometry.

• Authors: Inga Petry , Jacek R Wiśniewski , Zbigniew Szewczuk
• Languages of publication: EN

Abstracts

EN

The high mobility group (HMG) proteins are abundant non-histone components of eukaryotic chromatin. The presence of C-terminal acidic tails is a common feature of the majority of HMG proteins. Although the biological significance of the acidic domains is not clear, they are conferring conformational and metabolic stability to the proteins in vitro. Moreover, the length and net charge of the acidic tails affect the strength of HMG protein interaction with DNA. Synthesis of an insect HMG protein by standard recombinant technology in bacteria leads to a mixture of the intact protein (cHMG1a-(1-113) (I)) and a series of its degradation products truncated at the C tail: cHMG1a-(1-111) (II); cHMG1a-(1-110) (III); cHMG1a-(1-109) (IV); cHMG1a-(1-108) (V); cHMG1a-(1-107) (VI); cHMG1a-(1-106) (VII). The proteins differ from each other only by the number of amino-acid residues at the C-terminal tail. We used H/D exchange mass spectrometry to characterize the stability of the proteins directly in their mixture. The results show that the proteins I-V and VII have very similar conformations. The protein VI is less compact and exchanges its protons faster than the others. It may be concluded that the C-terminal tail influences the conformation of the cHMG1a protein and that individual residues in this part of the protein play a key role in its compactness.

Keywords

EN

cHMG1a; protein conformation; ESI-MS; isotope exchange

• Journal: Acta Biochimica Polonica
• Year: 2001
• Volume: 48
• Issue: 4
• Pages: 1131-1136

Dates

published

2001

received

2001-09-19

accepted

2001-11-26

Contributors

author

Inga Petry

• Faculty of Chemistry, University of Wrocław, Wrocław, Poland

author

Jacek R Wiśniewski

• Zoologisches Institut-Entwicklungsbiologie, Universität Göttingen, Göttingen, Germany

author

Zbigniew Szewczuk

• Faculty of Chemistry, University of Wrocław, Wrocław, Poland

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