HOME HELP FEEDBACK SUBSCRIPTIONS ARCHIVE ADVANCED SEARCH TABLE OF CONTENTS		QUICK SEARCH:   [advanced] Author: Keyword(s): Year:  Vol:  Page:

This Article Full Text Full Text (PDF) Alert me when this article is cited Alert me if a correction is posted Citation Map Services Similar articles in this journal Similar articles in PubMed Alert me to new issues of the journal Download to citation manager Citing Articles Citing Articles via HighWire Citing Articles via Google Scholar Google Scholar Articles by Hirano, W. Articles by Seiki, M. Search for Related Content PubMed PubMed Citation Articles by Hirano, W. Articles by Seiki, M.

Division of Cancer Cell Research, Institute of Medical Science, University of Tokyo, Minato-ku, Tokyo, 108-8639, Japan

MTCBP-1 was identified as a protein that binds the cytoplasmic tail of membrane-type 1 matrix metalloproteinase (MT1-MMP/MMP-14). Since MTCBP-1 has a putative ß-barrel structure, it is presumably a member of the recently proposed cupin superfamily that contains tremendously diverged functions of proteins in spite of their well-conserved ß-barrel structure. MTCBP-1 shows significant homology to the bacterial aci-reductone dioxygenase (ARD) in the cupin family, which is an enzyme in the methionine salvage pathway (MTA cycle). Since it is difficult to speculate the functions of cupin proteins simply based on their sequence homology, we examined whether the eukaryotic ARD homologs surely function in the methionine metabolism. Under sulfur-depleted conditions, yeast could grow when substrate of MTA cycle was provided. Disruption of the yeast ARD homolog, YMR009w gene, abolished ability of the cells to grow in this culture condition. Re-expression of either the YMR009w or MTCBP-1 gene restored the cell growth. Mutation analysis revealed that the glutamic acid residue in the ß-barrel fold and the N-terminal extension from the ß-barrel fold were found to be important for the activity to restore the growth. Thus, MTCBP-1 isolated as a binding protein for MT1-MMP was demonstrated to function as an ARD-like enzyme in the MTA cycle in yeast.

^aPresent address: Growth Factor Division, National Cancer Center Research Institute, Chuo-ku, Tokyo, 104-0045, Japan.

^* Correspondence: E-mail: mseiki{at}ims.u-tokyo.ac.jp

This article has been cited by other articles:

				M. Costa, C. L. Borges, A. M. Bailao, G. V. Meirelles, Y. A. Mendonca, S. F. I. M. Dantas, F. P. de Faria, M. S. S. Felipe, E. E. W. I. Molinari-Madlum, M. J. S. Mendes-Giannini, et al. Transcriptome profiling of Paracoccidioides brasiliensis yeast-phase cells recovered from infected mice brings new insights into fungal response upon host interaction Microbiology, December 1, 2007; 153(12): 4194 - 4207. [Abstract] [Full Text] [PDF]

				I. Gotoh, T. Uekita, and M. Seiki Regulated nucleo-cytoplasmic shuttling of human aci-reductone dioxygenase (hADI1) and its potential role in mRNA processing. Genes Cells, January 1, 2007; 12(1): 105 - 117. [Abstract] [Full Text] [PDF]