Purification, crystallization and initial X-ray diffraction study of human REV7 in complex with a REV3 fragment

Area of Science:

• Molecular Biology
• Structural Biology
• Biochemistry

Background:

• REV7 protein is essential for DNA replication, signal transduction, and cell-cycle regulation.
• REV7 collaborates with REV3 to form DNA polymerase zeta, a key enzyme in error-prone DNA synthesis.
• REV3, the catalytic subunit, has its activity enhanced by REV7.

Purpose of the Study:

• To elucidate the structural basis of the interaction between human REV7 and REV3.
• To provide atomic-level understanding of REV7-REV3 complex formation.

Main Methods:

• X-ray crystallography was employed to determine the structure of the human REV7-REV3 fragment complex.
• Two distinct crystal forms (Form I and Form II) were obtained and characterized.

Main Results:

• The study successfully crystallized the human REV7 protein in complex with a REV3 fragment.
• Crystal Form I belongs to space group P2(1) with specific unit-cell parameters.
• Crystal Form II belongs to space group P4(1)2(1)2 or P4(3)2(1)2 with distinct unit-cell parameters.

Conclusions:

• The structural data provides a foundation for understanding the functional interplay between REV7 and REV3.
• Insights into the REV7-REV3 interaction can inform future research on DNA repair and mutagenesis.