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HTTM, a horizontally transferred transmembrane domain.

Jörg Schultz¹

¹Computational Molecular Biology, Max-Planck-Institute for Molecular Genetics, Ihnestrasse 73, 14195 Berlin, Germany. Joerg.Schultz@biozentrum.uni-wuerzburg.de

Trends in Biochemical Sciences

|January 20, 2004

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A novel domain, horizontally transferred transmembrane (HTTM), was found in vitamin K-dependent gamma-carboxylases (VKGC). This transmembrane domain likely arose from horizontal gene transfer across diverse life forms.

Area of Science:

Biochemistry
Molecular Biology
Evolutionary Biology

Background:

Vitamin K-dependent gamma-carboxylases (VKGC) are enzymes crucial for post-translational modification.
Understanding the structural domains of VKGC is essential for elucidating their function and evolutionary history.

Purpose of the Study:

To identify and characterize novel domains within vitamin K-dependent gamma-carboxylases.
To investigate the evolutionary origin and distribution of these domains across different life domains.

Main Methods:

Sequence analysis of vitamin K-dependent gamma-carboxylases (VKGC) across various species.
Bioinformatic analysis to identify conserved domains and transmembrane regions.

Main Results:

Related Experiment Videos

A novel N-terminal domain, termed horizontally transferred transmembrane (HTTM), was identified in VKGC.
The HTTM domain contains four transmembrane regions, a unique feature among known protein domains.
The distribution of HTTM in eukaryotes, bacteria, and archaea suggests horizontal gene transfer as its origin, rather than early evolutionary divergence.

Conclusions:

The horizontally transferred transmembrane (HTTM) domain represents a significant finding in the study of vitamin K-dependent gamma-carboxylases.
The presence of HTTM across diverse taxa points to horizontal gene transfer as a major mechanism in shaping protein evolution.
Conservation of catalytic sites suggests enzymatic roles for other family members, warranting further investigation.