Abstract:
:The role of H211 of the yeast F1-ATPase beta-subunit was investigated by site-specific mutagenesis and characterization of the resulting enzymes. Five amino acids (N, D, I, K, and A) were substituted for H211 of the ATP2 gene. The mutated genes were expressed in an atp2::LEU2 host, and only yeast expressing H211N respired aerobically. The respiratory phenotypes of the other four mutants were suppressed by a second site mutation (L203F). The ATPases from the single mutant strains were unstable when removed from the mitochondrial inner membrane, preventing purification. Submitochondrial particles were prepared from each strain and the activities were stable under a variety of conditions, allowing determination of Vmax and Km for ATP hydrolysis. Mutations of H211 caused increases in Km of 3.7- to 7.4-fold, while L203F had little effect. The suppressive effect of the L203F mutation was also expressed in the Km values of the double mutant strains. The ATPases from the H211 mutants had diminished sensitivity to oligomycin, and their pH optima were 1.5-2.0 units less than the wild-type optimum. Values of pKa for the groups involved in catalysis were estimated for the wild-type enzyme and three H211 mutants (N, D, and K). Each mutant enzyme showed a substantial decrease in the pKa of the group(s) which serves as a base in acid-base catalysis. The results of this study demonstrate that H211 is important in maintaining the structure of the wild-type enzyme complex and also contributes to the structure of the active site. L203 is also required for the stability of the enzyme complex and may have a structural or functional interaction with H211. Neither H211 nor L203 is required for catalysis by F1.
journal_name
Arch Biochem Biophysjournal_title
Archives of biochemistry and biophysicsauthors
Schnizer RA,Schuster SMdoi
10.1006/abbi.1996.0056subject
Has Abstractpub_date
1996-02-01 00:00:00pages
126-36issue
1eissn
0003-9861issn
1096-0384pii
S0003-9861(96)90056-9journal_volume
326pub_type
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journal_title:Archives of biochemistry and biophysics
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doi:10.1016/0003-9861(84)90502-2
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更新日期:1995-05-10 00:00:00
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journal_title:Archives of biochemistry and biophysics
pub_type: 杂志文章
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journal_title:Archives of biochemistry and biophysics
pub_type: 杂志文章
doi:10.1006/abbi.1993.1527
更新日期:1993-11-01 00:00:00
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pub_type: 杂志文章
doi:10.1016/j.abb.2003.09.010
更新日期:2003-12-01 00:00:00
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更新日期:1989-09-01 00:00:00
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journal_title:Archives of biochemistry and biophysics
pub_type: 杂志文章
doi:10.1006/abbi.1995.0020
更新日期:1995-10-20 00:00:00
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journal_title:Archives of biochemistry and biophysics
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更新日期:2007-08-01 00:00:00
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journal_title:Archives of biochemistry and biophysics
pub_type: 杂志文章
doi:10.1006/abbi.2000.2059
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pub_type: 杂志文章
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journal_title:Archives of biochemistry and biophysics
pub_type: 杂志文章
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pub_type: 杂志文章
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pub_type: 杂志文章
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更新日期:2001-09-01 00:00:00
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journal_title:Archives of biochemistry and biophysics
pub_type: 杂志文章
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更新日期:2005-10-15 00:00:00
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pub_type: 杂志文章
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journal_title:Archives of biochemistry and biophysics
pub_type: 杂志文章
doi:10.1006/abbi.2000.1821
更新日期:2000-06-01 00:00:00
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journal_title:Archives of biochemistry and biophysics
pub_type: 杂志文章
doi:10.1016/0003-9861(91)90604-h
更新日期:1991-10-01 00:00:00