This Article Full Text (PDF) Alert me when this article is cited Alert me if a correction is posted Services Similar articles in this journal Similar articles in PubMed Alert me to new issues of the journal Download to citation manager Reprints and Permissions Copyright Information Books from ASM Press MicrobeWorld Citing Articles Citing Articles via HighWire Citing Articles via Google Scholar Google Scholar Articles by Kmiec, E B Articles by Holloman, W K Search for Related Content PubMed PubMed Citation Articles by Kmiec, E B Articles by Holloman, W K

The REC2 gene encodes the homologous pairing protein of Ustilago maydis.

Department of Pharmacology, Jefferson Cancer Center, Thomas Jefferson University, Philadelphia, Pennsylvania 19117.

ABSTRACT

Amino acid sequence analysis has established that the homologous pairing protein of Ustilago maydis, known previously in the literature as rec1, is encoded by REC2, a gene essential for recombinational repair and meiosis with regional homology to Escherichia coli RecA. The 70-kDa rec1 protein is most likely a proteolytic degradation product of REC2, which has a predicted mass of 84 kDa but which runs anomalously during sodium dodecyl sulfate-gel electrophoresis with an apparent mass of 110 kDa. To facilitate purification of the protein product, the REC2 gene was overexpressed from a vector that fused a hexahistidine leader sequence onto the amino terminus, enabling isolation of the REC2 protein on an immobilized metal affinity column. The purified protein exhibits ATP-dependent DNA renaturation and DNA-dependent ATPase activities, which were reactions characteristic of the protein as purified from cell extracts of U. maydis. Homologous pairing activity was established in an assay that measures recognition via non-Watson-Crick bonds between identical DNA strands. A size threshold of about 50 bp was found to govern pairing between linear duplex molecules and homologous single-stranded circles. Joint molecule formation with duplex DNA well under the size threshold was efficiently catalyzed when one strand of the duplex was composed of RNA. Linear duplex molecules with hairpin caps also formed joint molecules when as few as three RNA residues were present.

This article has been cited by other articles:

• Akhmedov, A. T., Lopez, B. S. (2000). Human 100-kDa homologous DNA-pairing protein is the splicing factor PSF and promotes DNA strand invasion. Nucleic Acids Res 28: 3022-3030 [Abstract] [Full Text]  
• Hedner, U., Ginsburg, D., Lusher, J. M., High, K. A. (2000). Congenital Hemorrhagic Disorders: New Insights into the Pathophysiology and Treatment of Hemophilia. ASH Education Book 2000: 241-265 [Abstract] [Full Text]  
• Baechtold, H., Kuroda, M., Sok, J., Ron, D., Lopez, B. S., Akhmedov, A. T. (1999). Human 75-kDa DNA-pairing Protein Is Identical to the Pro-oncoprotein TLS/FUS and Is Able to Promote D-loop Formation. J. Biol. Chem. 274: 34337-34342 [Abstract] [Full Text]  
• Kren, B. T., Parashar, B., Bandyopadhyay, P., Chowdhury, N. R., Chowdhury, J. R., Steer, C. J. (1999). Correction of the UDP-glucuronosyltransferase gene defect in the Gunn rat model of Crigler-Najjar syndrome type I with a chimeric oligonucleotide. Proc. Natl. Acad. Sci. USA 96: 10349-10354 [Abstract] [Full Text]  
• Hohn, B., Puchta, H. (1999). Gene therapy in plants. Proc. Natl. Acad. Sci. USA 96: 8321-8323 [Full Text]  
• Fan, G., Ma, X., Kren, B. T., Rice, M., Kmiec, E. B., Steer, C. J. (1997). A Novel Link Between REC2, a DNA Recombinase, the Retinoblastoma Protein, and Apoptosis. J. Biol. Chem. 272: 19413-19417 [Abstract] [Full Text]  
• Rice, M. C., Smith, S. T., Bullrich, F., Havre, P., Kmiec, E. B. (1997). Isolation of human and mouse genes based on homology to REC2, a recombinational repair gene from the fungus Ustilago maydis. Proc. Natl. Acad. Sci. USA 94: 7417-7422 [Abstract] [Full Text]  
• Cole-Strauss, A., Yoon, K., Xiang, Y., Byrne, B. C., Rice, M. C., Gryn, J., Holloman, W. K., Kmiec, E. B. (1996). Correction of the Mutation Responsible for Sickle Cell Anemia by an RNA-DNA Oligonucleotide. Science 273: 1386-1389 [Abstract]