Random mutagenesis of 1-aminocyclopropane-1-carboxylate synthase: a key enzyme in ethylene biosynthesis
1-Aminocyclopropane-1-carboxylate synthase (ACC synthase, EC 4.4.1.14) catalyzes the rate-limiting step in the ethylene biosynthetic pathway in plants. To determine the amino acid residues critical for the structure and function of this enzyme, the tomato Le-ACS2 isoenzyme has been subjected to both...
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Published in | Proceedings of the National Academy of Sciences - PNAS Vol. 95; no. 17; pp. 9796 - 9801 |
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Main Authors | , , |
Format | Journal Article |
Language | English |
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United States
National Academy of Sciences of the United States of America
18.08.1998
National Acad Sciences National Academy of Sciences |
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Abstract | 1-Aminocyclopropane-1-carboxylate synthase (ACC synthase, EC 4.4.1.14) catalyzes the rate-limiting step in the ethylene biosynthetic pathway in plants. To determine the amino acid residues critical for the structure and function of this enzyme, the tomato Le-ACS2 isoenzyme has been subjected to both site-directed and PCR random mutagenesis. Mutant ACC synthases with reduced enzyme activity have been selected by using a genetic screen based on the functional complementation of an Escherichia coli Ile auxotroph that has been engineered to express ACC deaminase from Pseudomonas sp. The DNA sequence of almost 1,000 clones has been determined, and 334 single missense mutations have been selected for analysis. We have identified three classes of mutants based on their activity and expression in E. coli. Class I and II mutants have the same level of protein expression as the wild type, but their enzyme activity is reduced to 0-5% and 5-50%, respectively. Class III mutants have neither activity nor detectable protein expression. The inactive mutations are clustered in regions that are highly conserved among various ACC synthases. This library of mutants will facilitate the elucidation of structure-function relationships of this regulatory enzyme |
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AbstractList | 1-Aminocyclopropane-1-carboxylate synthase (ACC synthase, EC 4.4.1.14) catalyzes the rate-limiting step in the ethylene biosynthetic pathway in plants. To determine the amino acid residues critical for the structure and function of this enzyme, the tomato Le-ACS2 isoenzyme has been subjected to both site-directed and PCR random mutagenesis. Mutant ACC synthases with reduced enzyme activity have been selected by using a genetic screen based on the functional complementation of an Escherichia coli Ile auxotroph that has been engineered to express ACC deaminase from Pseudomonas sp. The DNA sequence of almost 1,000 clones has been determined, and 334 single missense mutations have been selected for analysis. We have identified three classes of mutants based on their activity and expression in E. coli. Class I and II mutants have the same level of protein expression as the wild type, but their enzyme activity is reduced to 0-5% and 5-50%, respectively. Class III mutants have neither activity nor detectable protein expression. The inactive mutations are clustered in regions that are highly conserved among various ACC synthases. This library of mutants will facilitate the elucidation of structure-function relationships of this regulatory enzyme. 1-Aminocyclopropane-1-carboxylate synthase (ACC synthase, EC 4.4.1.14 ) catalyzes the rate-limiting step in the ethylene biosynthetic pathway in plants. To determine the amino acid residues critical for the structure and function of this enzyme, the tomato Le-ACS2 isoenzyme has been subjected to both site-directed and PCR random mutagenesis. Mutant ACC synthases with reduced enzyme activity have been selected by using a genetic screen based on the functional complementation of an Escherichia coli Ile auxotroph that has been engineered to express ACC deaminase from Pseudomonas sp. The DNA sequence of almost 1,000 clones has been determined, and 334 single missense mutations have been selected for analysis. We have identified three classes of mutants based on their activity and expression in E. coli. Class I and II mutants have the same level of protein expression as the wild type, but their enzyme activity is reduced to 0–5% and 5–50%, respectively. Class III mutants have neither activity nor detectable protein expression. The inactive mutations are clustered in regions that are highly conserved among various ACC synthases. This library of mutants will facilitate the elucidation of structure-function relationships of this regulatory enzyme. isoleucine auxotroph/missense mutation/growth screen/structure-function analysis 1-Aminocyclopropane-1-carboxylate synthase (ACC synthase, EC 4.4.1.14) catalyzes the rate-limiting step in the ethylene biosynthetic pathway in plants. To determine the amino acid residues critical for the structure and function of this enzyme, the tomato Le-ACS2 isoenzyme has been subjected to both site-directed and PCR random mutagenesis. 1-Aminocyclopropane-1-carboxylate synthase (ACC synthase, EC 4.4.1.14) catalyzes the rate-limiting step in the ethylene biosynthetic pathway in plants. To determine the amino acid residues critical for the structure and function of this enzyme, the tomato Le-ACS2 isoenzyme has been subjected to both site-directed and PCR random mutagenesis. Mutant ACC synthases with reduced enzyme activity have been selected by using a genetic screen based on the functional complementation of an Escherichia coli Ile auxotroph that has been engineered to express ACC deaminase from Pseudomonas sp. The DNA sequence of almost 1,000 clones has been determined, and 334 single missense mutations have been selected for analysis. We have identified three classes of mutants based on their activity and expression in E. coli. Class I and II mutants have the same level of protein expression as the wild type, but their enzyme activity is reduced to 0-5% and 5-50%, respectively. Class III mutants have neither activity nor detectable protein expression. The inactive mutations are clustered in regions that are highly conserved among various ACC synthases. This library of mutants will facilitate the elucidation of structure-function relationships of this regulatory enzyme 1-Aminocyclopropane-1-carboxylate synthase (ACC synthase, EC 4.4.1.14 ) catalyzes the rate-limiting step in the ethylene biosynthetic pathway in plants. To determine the amino acid residues critical for the structure and function of this enzyme, the tomato Le-ACS2 isoenzyme has been subjected to both site-directed and PCR random mutagenesis. Mutant ACC synthases with reduced enzyme activity have been selected by using a genetic screen based on the functional complementation of an Escherichia coli Ile auxotroph that has been engineered to express ACC deaminase from Pseudomonas sp. The DNA sequence of almost 1,000 clones has been determined, and 334 single missense mutations have been selected for analysis. We have identified three classes of mutants based on their activity and expression in E. coli. Class I and II mutants have the same level of protein expression as the wild type, but their enzyme activity is reduced to 0–5% and 5–50%, respectively. Class III mutants have neither activity nor detectable protein expression. The inactive mutations are clustered in regions that are highly conserved among various ACC synthases. This library of mutants will facilitate the elucidation of structure-function relationships of this regulatory enzyme. |
Author | Lee, J.S Tarun, A.S. (Plant Gene Expression Center, Albany, CA.) Theologis, A |
AuthorAffiliation | Plant Gene Expression Center, 800 Buchanan Street, Albany, CA 94710 |
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Author_xml | – sequence: 1 fullname: Tarun, A.S. (Plant Gene Expression Center, Albany, CA.) – sequence: 2 fullname: Lee, J.S – sequence: 3 fullname: Theologis, A |
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Cites_doi | 10.1006/jmbi.1994.1165 10.1016/0022-2836(91)90738-R 10.1016/0014-5793(95)01464-0 10.1073/pnas.89.22.11046 10.1006/jmbi.1993.1413 10.1016/0378-1119(95)00694-X 10.1038/339031a0 10.1021/bi00244a013 10.1016/0022-2836(90)90126-7 10.1002/prot.340190108 10.1073/pnas.91.26.12428 10.1006/bbrc.1994.1020 10.1021/bi971625l 10.1104/pp.91.3.1036 10.1006/jmbi.1994.1695 10.1021/bi00239a022 10.1016/S0021-9258(18)83275-6 10.1038/340397a0 10.1016/0022-2836(91)90587-V 10.1073/pnas.88.16.7021 10.1006/jmbi.1996.0279 10.1073/pnas.76.1.170 10.1002/pro.5560050516 10.1006/jmbi.1994.1458 10.1021/bi9528715 10.1016/0378-1119(94)90856-7 10.1002/prot.340200303 10.1146/annurev.pp.44.060193.001435 10.1073/pnas.82.23.7820 10.1007/BF00016491 10.1128/jb.65.2.203-209.1953 10.1007/BF00039554 10.1016/S0021-9258(19)67859-2 10.1074/jbc.273.20.12509 10.1111/j.1432-1033.1989.tb15202.x 10.1016/S0021-9258(17)37461-6 10.1006/jmbi.1997.0924 10.1006/abio.1995.1050 |
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References | Sambrook J (e_1_3_3_22_2) 1989 e_1_3_3_17_2 e_1_3_3_16_2 Rost B (e_1_3_3_29_2) 1995 e_1_3_3_19_2 e_1_3_3_38_2 e_1_3_3_18_2 e_1_3_3_39_2 e_1_3_3_13_2 e_1_3_3_36_2 e_1_3_3_12_2 e_1_3_3_37_2 e_1_3_3_15_2 e_1_3_3_34_2 e_1_3_3_14_2 e_1_3_3_35_2 e_1_3_3_32_2 e_1_3_3_33_2 e_1_3_3_11_2 e_1_3_3_30_2 e_1_3_3_10_2 e_1_3_3_31_2 Klee H J (e_1_3_3_20_2) 1991; 3 e_1_3_3_40_2 e_1_3_3_6_2 e_1_3_3_5_2 e_1_3_3_8_2 e_1_3_3_7_2 e_1_3_3_28_2 e_1_3_3_9_2 e_1_3_3_27_2 e_1_3_3_24_2 e_1_3_3_23_2 e_1_3_3_26_2 e_1_3_3_25_2 e_1_3_3_2_2 e_1_3_3_4_2 e_1_3_3_41_2 Abeles F B (e_1_3_3_1_2) 1992 e_1_3_3_3_2 e_1_3_3_21_2 e_1_3_3_42_2 |
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Snippet | 1-Aminocyclopropane-1-carboxylate synthase (ACC synthase, EC 4.4.1.14) catalyzes the rate-limiting step in the ethylene biosynthetic pathway in plants. To... 1-Aminocyclopropane-1-carboxylate synthase (ACC synthase, EC 4.4.1.14 ) catalyzes the rate-limiting step in the ethylene biosynthetic pathway in plants. To... 1-Aminocyclopropane-1-carboxylate synthase (ACC synthase, EC 4.4.1. 14) catalyzes the rate-limiting step in the ethylene biosynthetic pathway in plants. To... 1-Aminocyclopropane-1-carboxylate synthase (ACC synthase, EC 4.4.1.14 ) catalyzes the rate-limiting step in the ethylene biosynthetic pathway in plants. To... |
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SubjectTerms | ACC SYNTHASE ACTIVIDAD ENZIMATICA ACTIVITE ENZYMATIQUE ADN Amino Acid Sequence AMINO ACID SEQUENCES Amino acids Base Sequence Binding Sites - genetics Biochemistry Biological Sciences CHEMICAL COMPOSITION COMPLEMENTARY DNA COMPLEMENTATION COMPOSICION QUIMICA COMPOSITION CHIMIQUE DNA DNA Primers - genetics Enzymes ENZYMIC ACTIVITY ESCHERICHIA COLI Escherichia coli - enzymology Escherichia coli - genetics Ethylenes - biosynthesis Flowers & plants GENE Gene Expression GENES Genetic Complementation Test Genetic mutation Genetic screening GENETICA GENETICS GENETIQUE INDUCED MUTATION Isoenzymes - genetics Isoenzymes - metabolism ISOLEUCINE AUXOTROPHS LIASAS LYASE LYASES Lyases - genetics Lyases - metabolism LYCOPERSICON ESCULENTUM Lycopersicon esculentum - enzymology Lycopersicon esculentum - genetics MISSENSE MUTATIONS Molecular Sequence Data MUTACION MUTACION INDUCIDA Mutagenesis Mutagenesis, Site-Directed MUTANT MUTANTES MUTANTS MUTATION MUTATION PROVOQUEE PCR Plasmids POLYMERASE CHAIN REACTION Protein synthesis Pseudomonas Pseudomonas - enzymology Pseudomonas - genetics TARGETED MUTAGENESIS |
Title | Random mutagenesis of 1-aminocyclopropane-1-carboxylate synthase: a key enzyme in ethylene biosynthesis |
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