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A Loop in the N-terminal Region of MCM Mediates Communication With the Catalytic Domain

Published

Author(s)

Nozomi Sakakibara, Rajesh Kasiviswanathan, E Melamud, Frederick P. Schwarz, Z Kelman

Abstract

Minichromosome maintenance helicases are the presumptive replicative helicases, thought to separate the two strands of chromosomal DNA during replication. In archaea, the catalytic activity resides within the C-terminal region of the MCM protein. In Methanothermobacter themautotrophicus the N-terminal portion of the protein was shown to be involved in protein multimerization and binding to single and double stranded DNA. MCM homologues from many archaeal species have highly conserved predicted amino acid similarity in a loop located between b7 and b8 in the N-terminal part of the molecule. This high degree of conservation suggests a functional role for the loop. Mutational analysis of the conserved residues suggests that the loop participates in communication between the N-terminal portion of the helicase and the C-terminal catalytic domain. Since similar residues are also conserved in the eukaryotic MCM proteins, the data presented here suggest a similar coupling between the N-terminal and catalytic domain of the eukaryotic enzyme.
Citation
Journal of Biological Chemistry

Keywords

ATP, circular dichroism, differential scanning calorimetry, MCM helicases, replication

Citation

Sakakibara, N. , Kasiviswanathan, R. , Melamud, E. , Schwarz, F. and Kelman, Z. (2021), A Loop in the N-terminal Region of MCM Mediates Communication With the Catalytic Domain, Journal of Biological Chemistry (Accessed April 16, 2024)
Created October 12, 2021