Characterization of a new hemoprotein in the yeast Saccharomyces cerevisiae

被引:11
作者
Sartori, G
Aldegheri, L
Mazzotta, G
Lanfranchi, G
Tournu, H
Brown, AJP
Carignani, G
机构
[1] Univ Padua, Dipartimento Chim Biol, I-35121 Padua, Italy
[2] Univ Padua, Dipartimento Biol, I-35121 Padua, Italy
[3] Univ Aberdeen, Inst Med Sci, Aberdeen AB25 2ZD, Scotland
关键词
D O I
10.1074/jbc.274.8.5032
中图分类号
Q5 [生物化学]; Q7 [分子生物学];
学科分类号
071010 ; 081704 ;
摘要
The Saccharomyces cerevisiae gene YNL234w encodes a 426-amino acid-long protein that shares significant similarities with the globin family. Compared with known globins from unicellular organisms, the Ynl234wp polypeptide is characterized by an unusual structure. In this protein, a central putative heme-binding domain of about 140 amino acids is flanked by two sequences of about 160 and 120 amino acids, respectively, which share no similarity with known polypeptides. Northern analysis indicates that YNL234w transcription is very low in cells grown under normal aerobic conditions but is induced by oxygen-limited growth conditions and by other stress conditions such as glucose repression, heat shock, osmotic stress, and nitrogen starvation. However the deletion of the gene had no detectable effect on yeast growth. The Ynl234wp polypeptide has been expressed in Escherichia coli, and the hemoprotein nature of the recombinant protein was demonstrated by heme staining after SDS/polyacrylamide gel electrophoresis and spectroscopic analysis. Our data indicate that purified recombinant Ynl234wp possesses a noncovalently bound heme molecule that is predominantly found in a low spin form.
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页码:5032 / 5037
页数:6
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