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 Perozzi, G Articles by Prakash, S Search for Related Content PubMed PubMed Citation Articles by Perozzi, G Articles by Prakash, S

 Previous Article  |  Next Article 

Mol Cell Biol. 1986 May; 6(5): 1497-1507

RAD7 gene of Saccharomyces cerevisiae: transcripts, nucleotide sequence analysis, and functional relationship between the RAD7 and RAD23 gene products.

ABSTRACT

The RAD7 gene of Saccharomyces cerevisiae was cloned on a 4.0-kilobase (kb) DNA fragment and shown to provide full complementation of a rad7-delta mutant strain. The nucleotide sequence of a 2.2-kb DNA fragment which contains the complete RAD7 gene was determined. Transcription of the RAD7 gene initiates at multiple sites in a region spanning positions -61 to -8 of the DNA sequence. The 1.8-kb RAD7 mRNA encodes a protein of 565 amino acids with a predicted size of 63.7 kilodaltons. The hydropathy profile of the RAD7 protein indicates a highly hydrophilic amino terminus and a very hydrophobic region toward the carboxyl terminus. A RAD7 subclone deleted for the first 99 codons complements the rad7-delta mutation, but not the rad7-delta rad23-delta double mutation, indicating that the RAD23 protein can compensate for the function that is missing in the amino-terminally deleted RAD7 protein. The RAD7 and RAD23 genes in multicopy plasmids do not complement the rad23-delta and rad7-delta mutations, respectively. These observations could mean that although the two proteins might share a common functional domain, they must also perform distinct functions. Alternatively, an interaction between the RAD7 and RAD23 proteins could also account for these observations.

This article has been cited by other articles:

• Ortolan, T. G., Chen, L., Tongaonkar, P., Madura, K. (2004). Rad23 stabilizes Rad4 from degradation by the Ub/proteasome pathway. Nucleic Acids Res 32: 6490-6500 [Abstract] [Full Text]  
• Ramsey, K. L., Smith, J. J., Dasgupta, A., Maqani, N., Grant, P., Auble, D. T. (2004). The NEF4 Complex Regulates Rad4 Levels and Utilizes Snf2/Swi2-Related ATPase Activity for Nucleotide Excision Repair. Mol. Cell. Biol. 24: 6362-6378 [Abstract] [Full Text]  
• Rodriguez, K., Talamantez, J., Huang, W., Reed, S. H., Wang, Z., Chen, L., Feaver, W. J., Friedberg, E. C., Tomkinson, A. E. (1998). Affinity Purification and Partial Characterization of a Yeast Multiprotein Complex for Nucleotide Excision Repair Using Histidine-tagged Rad14 Protein. J. Biol. Chem. 273: 34180-34189 [Abstract] [Full Text]  
• Reardon, J. T., Mu, D., Sancar, A. (1996). Overproduction, Purification, and Characterization of the XPC Subunit of the Human DNA Repair Excision Nuclease. J. Biol. Chem. 271: 19451-19456 [Abstract] [Full Text]  
• Paetkau, D W, Riese, J A, MacMorran, W S, Woods, R A, Gietz, R D (1994). Interaction of the yeast RAD7 and SIR3 proteins: implications for DNA repair and chromatin structure.. Genes Dev. 8: 2035-2045 [Abstract]