On the Evolution of β -galactosidase
The amino acid sequence of β -galactosidase (β -D-galactoside galactohydrolase, EC 3.2.1.23) has been compared to itself and to other proteins. Two segments, each of about 380 amino acids, comprising the first three-fourths of the polypeptide chain, were found to be very similar to each other. It is...
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| Veröffentlicht in: | Proceedings of the National Academy of Sciences - PNAS 1978-01, Vol.75 (1), p.113-116 |
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| container_title | Proceedings of the National Academy of Sciences - PNAS |
| container_volume | 75 |
| creator | Hood, J. Myron Fowler, Audree V. Zabin, Irving |
| description | The amino acid sequence of β -galactosidase (β -D-galactoside galactohydrolase, EC 3.2.1.23) has been compared to itself and to other proteins. Two segments, each of about 380 amino acids, comprising the first three-fourths of the polypeptide chain, were found to be very similar to each other. It is concluded that they are homologous. The carboxyl-terminal fourth has a high percentage of amino acid identities with dihydrofolate reductase of Escherichia coli, suggesting these sequences also are homologous. A model for the origin of β -galactosidase is presented. The overall similarity of β -galactosidase to lac repressor does not appear to be significant. |
| doi_str_mv | 10.1073/pnas.75.1.113 |
| format | Article |
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The overall similarity of β -galactosidase to lac repressor does not appear to be significant.</description><identifier>ISSN: 0027-8424</identifier><identifier>EISSN: 1091-6490</identifier><identifier>DOI: 10.1073/pnas.75.1.113</identifier><identifier>PMID: 415304</identifier><language>eng</language><publisher>United States: National Academy of Sciences of the United States of America</publisher><subject>Amino Acid Sequence ; Amino acids ; Bacterial Proteins - genetics ; beta-Galactosidase - genetics ; Biochemistry ; Biological Evolution ; Enzyme Repression ; Escherichia coli - enzymology ; Escherichia coli - genetics ; Evolution ; Galactosidases - genetics ; Genes, Regulator ; Lac operon ; Lactose - metabolism ; Operon ; Operons ; Regional identity ; Repressor proteins ; rev genes ; Tetrahydrofolate Dehydrogenase - genetics</subject><ispartof>Proceedings of the National Academy of Sciences - PNAS, 1978-01, Vol.75 (1), p.113-116</ispartof><lds50>peer_reviewed</lds50><oa>free_for_read</oa><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c450t-58e6a8aa8ba4e606ae89e2581075e4073a003664b882c8cca2051458d77448fe3</citedby></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Uhttp://www.pnas.org/content/75/1.cover.gif</thumbnail><linktopdf>$$Uhttps://www.jstor.org/stable/pdf/67586$$EPDF$$P50$$Gjstor$$H</linktopdf><linktohtml>$$Uhttps://www.jstor.org/stable/67586$$EHTML$$P50$$Gjstor$$H</linktohtml><link.rule.ids>230,314,723,776,780,799,881,27901,27902,53766,53768,57992,58225</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/415304$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Hood, J. Myron</creatorcontrib><creatorcontrib>Fowler, Audree V.</creatorcontrib><creatorcontrib>Zabin, Irving</creatorcontrib><title>On the Evolution of β -galactosidase</title><title>Proceedings of the National Academy of Sciences - PNAS</title><addtitle>Proc Natl Acad Sci U S A</addtitle><description>The amino acid sequence of β -galactosidase (β -D-galactoside galactohydrolase, EC 3.2.1.23) has been compared to itself and to other proteins. Two segments, each of about 380 amino acids, comprising the first three-fourths of the polypeptide chain, were found to be very similar to each other. It is concluded that they are homologous. The carboxyl-terminal fourth has a high percentage of amino acid identities with dihydrofolate reductase of Escherichia coli, suggesting these sequences also are homologous. A model for the origin of β -galactosidase is presented. The overall similarity of β -galactosidase to lac repressor does not appear to be significant.</description><subject>Amino Acid Sequence</subject><subject>Amino acids</subject><subject>Bacterial Proteins - genetics</subject><subject>beta-Galactosidase - genetics</subject><subject>Biochemistry</subject><subject>Biological Evolution</subject><subject>Enzyme Repression</subject><subject>Escherichia coli - enzymology</subject><subject>Escherichia coli - genetics</subject><subject>Evolution</subject><subject>Galactosidases - genetics</subject><subject>Genes, Regulator</subject><subject>Lac operon</subject><subject>Lactose - metabolism</subject><subject>Operon</subject><subject>Operons</subject><subject>Regional identity</subject><subject>Repressor proteins</subject><subject>rev genes</subject><subject>Tetrahydrofolate Dehydrogenase - genetics</subject><issn>0027-8424</issn><issn>1091-6490</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>1978</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNptkLtOwzAYhS3ErRRGFsSQpWwJv-NrBgZUlYtUqQvMlps6bSo3LrFTwWvxIDwTqXpRkZg8fN_5fXQQusaQYBDkfllpnwiW4ARjcoQ6GDIcc5rBMeoApCKWNKXn6ML7OQBkTMIZOqWYEaAd1BtVUZiZaLBytgmlqyJXRD_fUTzVVufB-XKivblEJ4W23lxt3y56fxq89V_i4ej5tf84jHPKIMRMGq6l1nKsqeHAtZGZSZlsazJD264agHBOx1KmucxznQLDlMmJEJTKwpAuetjcXTbjhZnkpgq1tmpZlwtdfymnS_WXVOVMTd1KUYxxRtv83TZfu4_G-KAWpc-NtboyrvFKEilSkuJWjDdiXjvva1Ps_8Cg1quq9apKMIVVu2rr3x4W29ubGVvc2-J1agd3aVU01gbzGQ7O_Oe1-GaD5z64es-5YJKTXyYNknU</recordid><startdate>19780101</startdate><enddate>19780101</enddate><creator>Hood, J. 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Myron ; Fowler, Audree V. ; Zabin, Irving</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c450t-58e6a8aa8ba4e606ae89e2581075e4073a003664b882c8cca2051458d77448fe3</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>1978</creationdate><topic>Amino Acid Sequence</topic><topic>Amino acids</topic><topic>Bacterial Proteins - genetics</topic><topic>beta-Galactosidase - genetics</topic><topic>Biochemistry</topic><topic>Biological Evolution</topic><topic>Enzyme Repression</topic><topic>Escherichia coli - enzymology</topic><topic>Escherichia coli - genetics</topic><topic>Evolution</topic><topic>Galactosidases - genetics</topic><topic>Genes, Regulator</topic><topic>Lac operon</topic><topic>Lactose - metabolism</topic><topic>Operon</topic><topic>Operons</topic><topic>Regional identity</topic><topic>Repressor proteins</topic><topic>rev genes</topic><topic>Tetrahydrofolate Dehydrogenase - genetics</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Hood, J. Myron</creatorcontrib><creatorcontrib>Fowler, Audree V.</creatorcontrib><creatorcontrib>Zabin, Irving</creatorcontrib><collection>Medline</collection><collection>MEDLINE</collection><collection>MEDLINE (Ovid)</collection><collection>MEDLINE</collection><collection>MEDLINE</collection><collection>PubMed</collection><collection>CrossRef</collection><collection>MEDLINE - Academic</collection><collection>PubMed Central (Full Participant titles)</collection><jtitle>Proceedings of the National Academy of Sciences - PNAS</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Hood, J. Myron</au><au>Fowler, Audree V.</au><au>Zabin, Irving</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>On the Evolution of β -galactosidase</atitle><jtitle>Proceedings of the National Academy of Sciences - PNAS</jtitle><addtitle>Proc Natl Acad Sci U S A</addtitle><date>1978-01-01</date><risdate>1978</risdate><volume>75</volume><issue>1</issue><spage>113</spage><epage>116</epage><pages>113-116</pages><issn>0027-8424</issn><eissn>1091-6490</eissn><abstract>The amino acid sequence of β -galactosidase (β -D-galactoside galactohydrolase, EC 3.2.1.23) has been compared to itself and to other proteins. Two segments, each of about 380 amino acids, comprising the first three-fourths of the polypeptide chain, were found to be very similar to each other. It is concluded that they are homologous. The carboxyl-terminal fourth has a high percentage of amino acid identities with dihydrofolate reductase of Escherichia coli, suggesting these sequences also are homologous. A model for the origin of β -galactosidase is presented. The overall similarity of β -galactosidase to lac repressor does not appear to be significant.</abstract><cop>United States</cop><pub>National Academy of Sciences of the United States of America</pub><pmid>415304</pmid><doi>10.1073/pnas.75.1.113</doi><tpages>4</tpages><oa>free_for_read</oa></addata></record> |
| fulltext | fulltext |
| identifier | ISSN: 0027-8424 |
| ispartof | Proceedings of the National Academy of Sciences - PNAS, 1978-01, Vol.75 (1), p.113-116 |
| issn | 0027-8424 1091-6490 |
| language | eng |
| recordid | cdi_pubmedcentral_primary_oai_pubmedcentral_nih_gov_411194 |
| source | Jstor Complete Legacy; MEDLINE; PubMed Central; Alma/SFX Local Collection; Free Full-Text Journals in Chemistry |
| subjects | Amino Acid Sequence Amino acids Bacterial Proteins - genetics beta-Galactosidase - genetics Biochemistry Biological Evolution Enzyme Repression Escherichia coli - enzymology Escherichia coli - genetics Evolution Galactosidases - genetics Genes, Regulator Lac operon Lactose - metabolism Operon Operons Regional identity Repressor proteins rev genes Tetrahydrofolate Dehydrogenase - genetics |
| title | On the Evolution of β -galactosidase |
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