Evolution of the proteinase inhibitor I family and apparent lack of hypervariability in the proteinase contact loop
Abstract A protein phylogenetic tree was constructed from 24 homologous proteinase inhibitor I sequences identified in the EMBUGenbank and Swiss-Prot databases and from translated amino acid data from four constitutive cDNA clones of proteinase inhibitor I characterized from potato tuber mRNA. The t...
Ausführliche Beschreibung
Gespeichert in:
| Autor*in: |
|---|
| Format: |
E-Artikel |
|---|---|
| Sprache: |
Englisch |
| Erschienen: |
1994 |
|---|
| Umfang: |
11 |
|---|
| Reproduktion: |
Springer Online Journal Archives 1860-2002 |
|---|---|
| Übergeordnetes Werk: |
in: Journal of molecular evolution - 1971, 39(1994) vom: Juni, Seite 644-654 |
| Übergeordnetes Werk: |
volume:39 ; year:1994 ; month:06 ; pages:644-654 ; extent:11 |
| Links: |
|---|
| Katalog-ID: |
NLEJ20710042X |
|---|
| LEADER | 01000caa a22002652 4500 | ||
|---|---|---|---|
| 001 | NLEJ20710042X | ||
| 003 | DE-627 | ||
| 005 | 20210706221051.0 | ||
| 007 | cr uuu---uuuuu | ||
| 008 | 070528s1994 xx |||||o 00| ||eng c | ||
| 035 | |a (DE-627)NLEJ20710042X | ||
| 040 | |a DE-627 |b ger |c DE-627 |e rakwb | ||
| 041 | |a eng | ||
| 245 | 1 | 0 | |a Evolution of the proteinase inhibitor I family and apparent lack of hypervariability in the proteinase contact loop |
| 264 | 1 | |c 1994 | |
| 300 | |a 11 | ||
| 336 | |a nicht spezifiziert |b zzz |2 rdacontent | ||
| 337 | |a nicht spezifiziert |b z |2 rdamedia | ||
| 338 | |a nicht spezifiziert |b zu |2 rdacarrier | ||
| 520 | |a Abstract A protein phylogenetic tree was constructed from 24 homologous proteinase inhibitor I sequences identified in the EMBUGenbank and Swiss-Prot databases and from translated amino acid data from four constitutive cDNA clones of proteinase inhibitor I characterized from potato tuber mRNA. The tree suggests that divergence of at least four paralogous proteins with functional specialization occurred at different times during the evolutionary history of the proteinase inhibitor I family. Five distinct regions in the primary structure, earlier identified by structural studies, were used to analyze the inhibitor family for hypervariability (Creighton and Darby, Trends Biochem Sci 14:319–324, 1989). Mutations did not occur with higher-than-random frequency within the proteinase binding region. When isoinhibitor, orthologous, or paralogous data subsets were subsequently analyzed the same results were obtained. Comparison of the amino acid sequences for all the known potato proteinase isoinhibitor I proteins identified ten highly variable sites. These also were distributed randomly. Thus hypervariability, which has been observed in all other serine proteinase inhibitor families to date, appears to be lacking in the proteinase inhibitor I family. | ||
| 533 | |f Springer Online Journal Archives 1860-2002 | ||
| 700 | 1 | |a Beuning, Lesley L. |4 oth | |
| 700 | 1 | |a Spriggs, Thomas W. |4 oth | |
| 700 | 1 | |a Christeller, John T. |4 oth | |
| 773 | 0 | 8 | |i in |t Journal of molecular evolution |d 1971 |g 39(1994) vom: Juni, Seite 644-654 |w (DE-627)NLEJ188994645 |w (DE-600)1464309-1 |x 1432-1432 |7 nnns |
| 773 | 1 | 8 | |g volume:39 |g year:1994 |g month:06 |g pages:644-654 |g extent:11 |
| 856 | 4 | 0 | |u http://dx.doi.org/10.1007/BF00160410 |
| 912 | |a GBV_USEFLAG_U | ||
| 912 | |a ZDB-1-SOJ | ||
| 912 | |a GBV_NL_ARTICLE | ||
| 951 | |a AR | ||
| 952 | |d 39 |j 1994 |c 6 |h 644-654 |g 11 | ||
| matchkey_str |
article:14321432:1994----::vltootertiaeniioiaiynaprnlcohpraiblt |
|---|---|
| hierarchy_sort_str |
1994 |
| publishDate |
1994 |
| allfields |
(DE-627)NLEJ20710042X DE-627 ger DE-627 rakwb eng Evolution of the proteinase inhibitor I family and apparent lack of hypervariability in the proteinase contact loop 1994 11 nicht spezifiziert zzz rdacontent nicht spezifiziert z rdamedia nicht spezifiziert zu rdacarrier Abstract A protein phylogenetic tree was constructed from 24 homologous proteinase inhibitor I sequences identified in the EMBUGenbank and Swiss-Prot databases and from translated amino acid data from four constitutive cDNA clones of proteinase inhibitor I characterized from potato tuber mRNA. The tree suggests that divergence of at least four paralogous proteins with functional specialization occurred at different times during the evolutionary history of the proteinase inhibitor I family. Five distinct regions in the primary structure, earlier identified by structural studies, were used to analyze the inhibitor family for hypervariability (Creighton and Darby, Trends Biochem Sci 14:319–324, 1989). Mutations did not occur with higher-than-random frequency within the proteinase binding region. When isoinhibitor, orthologous, or paralogous data subsets were subsequently analyzed the same results were obtained. Comparison of the amino acid sequences for all the known potato proteinase isoinhibitor I proteins identified ten highly variable sites. These also were distributed randomly. Thus hypervariability, which has been observed in all other serine proteinase inhibitor families to date, appears to be lacking in the proteinase inhibitor I family. Springer Online Journal Archives 1860-2002 Beuning, Lesley L. oth Spriggs, Thomas W. oth Christeller, John T. oth in Journal of molecular evolution 1971 39(1994) vom: Juni, Seite 644-654 (DE-627)NLEJ188994645 (DE-600)1464309-1 1432-1432 nnns volume:39 year:1994 month:06 pages:644-654 extent:11 http://dx.doi.org/10.1007/BF00160410 GBV_USEFLAG_U ZDB-1-SOJ GBV_NL_ARTICLE AR 39 1994 6 644-654 11 |
| spelling |
(DE-627)NLEJ20710042X DE-627 ger DE-627 rakwb eng Evolution of the proteinase inhibitor I family and apparent lack of hypervariability in the proteinase contact loop 1994 11 nicht spezifiziert zzz rdacontent nicht spezifiziert z rdamedia nicht spezifiziert zu rdacarrier Abstract A protein phylogenetic tree was constructed from 24 homologous proteinase inhibitor I sequences identified in the EMBUGenbank and Swiss-Prot databases and from translated amino acid data from four constitutive cDNA clones of proteinase inhibitor I characterized from potato tuber mRNA. The tree suggests that divergence of at least four paralogous proteins with functional specialization occurred at different times during the evolutionary history of the proteinase inhibitor I family. Five distinct regions in the primary structure, earlier identified by structural studies, were used to analyze the inhibitor family for hypervariability (Creighton and Darby, Trends Biochem Sci 14:319–324, 1989). Mutations did not occur with higher-than-random frequency within the proteinase binding region. When isoinhibitor, orthologous, or paralogous data subsets were subsequently analyzed the same results were obtained. Comparison of the amino acid sequences for all the known potato proteinase isoinhibitor I proteins identified ten highly variable sites. These also were distributed randomly. Thus hypervariability, which has been observed in all other serine proteinase inhibitor families to date, appears to be lacking in the proteinase inhibitor I family. Springer Online Journal Archives 1860-2002 Beuning, Lesley L. oth Spriggs, Thomas W. oth Christeller, John T. oth in Journal of molecular evolution 1971 39(1994) vom: Juni, Seite 644-654 (DE-627)NLEJ188994645 (DE-600)1464309-1 1432-1432 nnns volume:39 year:1994 month:06 pages:644-654 extent:11 http://dx.doi.org/10.1007/BF00160410 GBV_USEFLAG_U ZDB-1-SOJ GBV_NL_ARTICLE AR 39 1994 6 644-654 11 |
| allfields_unstemmed |
(DE-627)NLEJ20710042X DE-627 ger DE-627 rakwb eng Evolution of the proteinase inhibitor I family and apparent lack of hypervariability in the proteinase contact loop 1994 11 nicht spezifiziert zzz rdacontent nicht spezifiziert z rdamedia nicht spezifiziert zu rdacarrier Abstract A protein phylogenetic tree was constructed from 24 homologous proteinase inhibitor I sequences identified in the EMBUGenbank and Swiss-Prot databases and from translated amino acid data from four constitutive cDNA clones of proteinase inhibitor I characterized from potato tuber mRNA. The tree suggests that divergence of at least four paralogous proteins with functional specialization occurred at different times during the evolutionary history of the proteinase inhibitor I family. Five distinct regions in the primary structure, earlier identified by structural studies, were used to analyze the inhibitor family for hypervariability (Creighton and Darby, Trends Biochem Sci 14:319–324, 1989). Mutations did not occur with higher-than-random frequency within the proteinase binding region. When isoinhibitor, orthologous, or paralogous data subsets were subsequently analyzed the same results were obtained. Comparison of the amino acid sequences for all the known potato proteinase isoinhibitor I proteins identified ten highly variable sites. These also were distributed randomly. Thus hypervariability, which has been observed in all other serine proteinase inhibitor families to date, appears to be lacking in the proteinase inhibitor I family. Springer Online Journal Archives 1860-2002 Beuning, Lesley L. oth Spriggs, Thomas W. oth Christeller, John T. oth in Journal of molecular evolution 1971 39(1994) vom: Juni, Seite 644-654 (DE-627)NLEJ188994645 (DE-600)1464309-1 1432-1432 nnns volume:39 year:1994 month:06 pages:644-654 extent:11 http://dx.doi.org/10.1007/BF00160410 GBV_USEFLAG_U ZDB-1-SOJ GBV_NL_ARTICLE AR 39 1994 6 644-654 11 |
| allfieldsGer |
(DE-627)NLEJ20710042X DE-627 ger DE-627 rakwb eng Evolution of the proteinase inhibitor I family and apparent lack of hypervariability in the proteinase contact loop 1994 11 nicht spezifiziert zzz rdacontent nicht spezifiziert z rdamedia nicht spezifiziert zu rdacarrier Abstract A protein phylogenetic tree was constructed from 24 homologous proteinase inhibitor I sequences identified in the EMBUGenbank and Swiss-Prot databases and from translated amino acid data from four constitutive cDNA clones of proteinase inhibitor I characterized from potato tuber mRNA. The tree suggests that divergence of at least four paralogous proteins with functional specialization occurred at different times during the evolutionary history of the proteinase inhibitor I family. Five distinct regions in the primary structure, earlier identified by structural studies, were used to analyze the inhibitor family for hypervariability (Creighton and Darby, Trends Biochem Sci 14:319–324, 1989). Mutations did not occur with higher-than-random frequency within the proteinase binding region. When isoinhibitor, orthologous, or paralogous data subsets were subsequently analyzed the same results were obtained. Comparison of the amino acid sequences for all the known potato proteinase isoinhibitor I proteins identified ten highly variable sites. These also were distributed randomly. Thus hypervariability, which has been observed in all other serine proteinase inhibitor families to date, appears to be lacking in the proteinase inhibitor I family. Springer Online Journal Archives 1860-2002 Beuning, Lesley L. oth Spriggs, Thomas W. oth Christeller, John T. oth in Journal of molecular evolution 1971 39(1994) vom: Juni, Seite 644-654 (DE-627)NLEJ188994645 (DE-600)1464309-1 1432-1432 nnns volume:39 year:1994 month:06 pages:644-654 extent:11 http://dx.doi.org/10.1007/BF00160410 GBV_USEFLAG_U ZDB-1-SOJ GBV_NL_ARTICLE AR 39 1994 6 644-654 11 |
| allfieldsSound |
(DE-627)NLEJ20710042X DE-627 ger DE-627 rakwb eng Evolution of the proteinase inhibitor I family and apparent lack of hypervariability in the proteinase contact loop 1994 11 nicht spezifiziert zzz rdacontent nicht spezifiziert z rdamedia nicht spezifiziert zu rdacarrier Abstract A protein phylogenetic tree was constructed from 24 homologous proteinase inhibitor I sequences identified in the EMBUGenbank and Swiss-Prot databases and from translated amino acid data from four constitutive cDNA clones of proteinase inhibitor I characterized from potato tuber mRNA. The tree suggests that divergence of at least four paralogous proteins with functional specialization occurred at different times during the evolutionary history of the proteinase inhibitor I family. Five distinct regions in the primary structure, earlier identified by structural studies, were used to analyze the inhibitor family for hypervariability (Creighton and Darby, Trends Biochem Sci 14:319–324, 1989). Mutations did not occur with higher-than-random frequency within the proteinase binding region. When isoinhibitor, orthologous, or paralogous data subsets were subsequently analyzed the same results were obtained. Comparison of the amino acid sequences for all the known potato proteinase isoinhibitor I proteins identified ten highly variable sites. These also were distributed randomly. Thus hypervariability, which has been observed in all other serine proteinase inhibitor families to date, appears to be lacking in the proteinase inhibitor I family. Springer Online Journal Archives 1860-2002 Beuning, Lesley L. oth Spriggs, Thomas W. oth Christeller, John T. oth in Journal of molecular evolution 1971 39(1994) vom: Juni, Seite 644-654 (DE-627)NLEJ188994645 (DE-600)1464309-1 1432-1432 nnns volume:39 year:1994 month:06 pages:644-654 extent:11 http://dx.doi.org/10.1007/BF00160410 GBV_USEFLAG_U ZDB-1-SOJ GBV_NL_ARTICLE AR 39 1994 6 644-654 11 |
| language |
English |
| source |
in Journal of molecular evolution 39(1994) vom: Juni, Seite 644-654 volume:39 year:1994 month:06 pages:644-654 extent:11 |
| sourceStr |
in Journal of molecular evolution 39(1994) vom: Juni, Seite 644-654 volume:39 year:1994 month:06 pages:644-654 extent:11 |
| format_phy_str_mv |
Article |
| institution |
findex.gbv.de |
| isfreeaccess_bool |
false |
| container_title |
Journal of molecular evolution |
| authorswithroles_txt_mv |
Beuning, Lesley L. @@oth@@ Spriggs, Thomas W. @@oth@@ Christeller, John T. @@oth@@ |
| publishDateDaySort_date |
1994-06-01T00:00:00Z |
| hierarchy_top_id |
NLEJ188994645 |
| id |
NLEJ20710042X |
| language_de |
englisch |
| fullrecord |
<?xml version="1.0" encoding="UTF-8"?><collection xmlns="http://www.loc.gov/MARC21/slim"><record><leader>01000caa a22002652 4500</leader><controlfield tag="001">NLEJ20710042X</controlfield><controlfield tag="003">DE-627</controlfield><controlfield tag="005">20210706221051.0</controlfield><controlfield tag="007">cr uuu---uuuuu</controlfield><controlfield tag="008">070528s1994 xx |||||o 00| ||eng c</controlfield><datafield tag="035" ind1=" " ind2=" "><subfield code="a">(DE-627)NLEJ20710042X</subfield></datafield><datafield tag="040" ind1=" " ind2=" "><subfield code="a">DE-627</subfield><subfield code="b">ger</subfield><subfield code="c">DE-627</subfield><subfield code="e">rakwb</subfield></datafield><datafield tag="041" ind1=" " ind2=" "><subfield code="a">eng</subfield></datafield><datafield tag="245" ind1="1" ind2="0"><subfield code="a">Evolution of the proteinase inhibitor I family and apparent lack of hypervariability in the proteinase contact loop</subfield></datafield><datafield tag="264" ind1=" " ind2="1"><subfield code="c">1994</subfield></datafield><datafield tag="300" ind1=" " ind2=" "><subfield code="a">11</subfield></datafield><datafield tag="336" ind1=" " ind2=" "><subfield code="a">nicht spezifiziert</subfield><subfield code="b">zzz</subfield><subfield code="2">rdacontent</subfield></datafield><datafield tag="337" ind1=" " ind2=" "><subfield code="a">nicht spezifiziert</subfield><subfield code="b">z</subfield><subfield code="2">rdamedia</subfield></datafield><datafield tag="338" ind1=" " ind2=" "><subfield code="a">nicht spezifiziert</subfield><subfield code="b">zu</subfield><subfield code="2">rdacarrier</subfield></datafield><datafield tag="520" ind1=" " ind2=" "><subfield code="a">Abstract A protein phylogenetic tree was constructed from 24 homologous proteinase inhibitor I sequences identified in the EMBUGenbank and Swiss-Prot databases and from translated amino acid data from four constitutive cDNA clones of proteinase inhibitor I characterized from potato tuber mRNA. The tree suggests that divergence of at least four paralogous proteins with functional specialization occurred at different times during the evolutionary history of the proteinase inhibitor I family. Five distinct regions in the primary structure, earlier identified by structural studies, were used to analyze the inhibitor family for hypervariability (Creighton and Darby, Trends Biochem Sci 14:319–324, 1989). Mutations did not occur with higher-than-random frequency within the proteinase binding region. When isoinhibitor, orthologous, or paralogous data subsets were subsequently analyzed the same results were obtained. Comparison of the amino acid sequences for all the known potato proteinase isoinhibitor I proteins identified ten highly variable sites. These also were distributed randomly. Thus hypervariability, which has been observed in all other serine proteinase inhibitor families to date, appears to be lacking in the proteinase inhibitor I family.</subfield></datafield><datafield tag="533" ind1=" " ind2=" "><subfield code="f">Springer Online Journal Archives 1860-2002</subfield></datafield><datafield tag="700" ind1="1" ind2=" "><subfield code="a">Beuning, Lesley L.</subfield><subfield code="4">oth</subfield></datafield><datafield tag="700" ind1="1" ind2=" "><subfield code="a">Spriggs, Thomas W.</subfield><subfield code="4">oth</subfield></datafield><datafield tag="700" ind1="1" ind2=" "><subfield code="a">Christeller, John T.</subfield><subfield code="4">oth</subfield></datafield><datafield tag="773" ind1="0" ind2="8"><subfield code="i">in</subfield><subfield code="t">Journal of molecular evolution</subfield><subfield code="d">1971</subfield><subfield code="g">39(1994) vom: Juni, Seite 644-654</subfield><subfield code="w">(DE-627)NLEJ188994645</subfield><subfield code="w">(DE-600)1464309-1</subfield><subfield code="x">1432-1432</subfield><subfield code="7">nnns</subfield></datafield><datafield tag="773" ind1="1" ind2="8"><subfield code="g">volume:39</subfield><subfield code="g">year:1994</subfield><subfield code="g">month:06</subfield><subfield code="g">pages:644-654</subfield><subfield code="g">extent:11</subfield></datafield><datafield tag="856" ind1="4" ind2="0"><subfield code="u">http://dx.doi.org/10.1007/BF00160410</subfield></datafield><datafield tag="912" ind1=" " ind2=" "><subfield code="a">GBV_USEFLAG_U</subfield></datafield><datafield tag="912" ind1=" " ind2=" "><subfield code="a">ZDB-1-SOJ</subfield></datafield><datafield tag="912" ind1=" " ind2=" "><subfield code="a">GBV_NL_ARTICLE</subfield></datafield><datafield tag="951" ind1=" " ind2=" "><subfield code="a">AR</subfield></datafield><datafield tag="952" ind1=" " ind2=" "><subfield code="d">39</subfield><subfield code="j">1994</subfield><subfield code="c">6</subfield><subfield code="h">644-654</subfield><subfield code="g">11</subfield></datafield></record></collection>
|
| series2 |
Springer Online Journal Archives 1860-2002 |
| ppnlink_with_tag_str_mv |
@@773@@(DE-627)NLEJ188994645 |
| format |
electronic Article |
| delete_txt_mv |
keep |
| collection |
NL |
| remote_str |
true |
| illustrated |
Not Illustrated |
| issn |
1432-1432 |
| topic_title |
Evolution of the proteinase inhibitor I family and apparent lack of hypervariability in the proteinase contact loop |
| format_facet |
Elektronische Aufsätze Aufsätze Elektronische Ressource |
| format_main_str_mv |
Text Zeitschrift/Artikel |
| carriertype_str_mv |
zu |
| author2_variant |
l l b ll llb t w s tw tws j t c jt jtc |
| hierarchy_parent_title |
Journal of molecular evolution |
| hierarchy_parent_id |
NLEJ188994645 |
| hierarchy_top_title |
Journal of molecular evolution |
| isfreeaccess_txt |
false |
| familylinks_str_mv |
(DE-627)NLEJ188994645 (DE-600)1464309-1 |
| title |
Evolution of the proteinase inhibitor I family and apparent lack of hypervariability in the proteinase contact loop |
| spellingShingle |
Evolution of the proteinase inhibitor I family and apparent lack of hypervariability in the proteinase contact loop |
| ctrlnum |
(DE-627)NLEJ20710042X |
| title_full |
Evolution of the proteinase inhibitor I family and apparent lack of hypervariability in the proteinase contact loop |
| journal |
Journal of molecular evolution |
| journalStr |
Journal of molecular evolution |
| lang_code |
eng |
| isOA_bool |
false |
| recordtype |
marc |
| publishDateSort |
1994 |
| contenttype_str_mv |
zzz |
| container_start_page |
644 |
| container_volume |
39 |
| physical |
11 |
| format_se |
Elektronische Aufsätze |
| title_sort |
evolution of the proteinase inhibitor i family and apparent lack of hypervariability in the proteinase contact loop |
| title_auth |
Evolution of the proteinase inhibitor I family and apparent lack of hypervariability in the proteinase contact loop |
| abstract |
Abstract A protein phylogenetic tree was constructed from 24 homologous proteinase inhibitor I sequences identified in the EMBUGenbank and Swiss-Prot databases and from translated amino acid data from four constitutive cDNA clones of proteinase inhibitor I characterized from potato tuber mRNA. The tree suggests that divergence of at least four paralogous proteins with functional specialization occurred at different times during the evolutionary history of the proteinase inhibitor I family. Five distinct regions in the primary structure, earlier identified by structural studies, were used to analyze the inhibitor family for hypervariability (Creighton and Darby, Trends Biochem Sci 14:319–324, 1989). Mutations did not occur with higher-than-random frequency within the proteinase binding region. When isoinhibitor, orthologous, or paralogous data subsets were subsequently analyzed the same results were obtained. Comparison of the amino acid sequences for all the known potato proteinase isoinhibitor I proteins identified ten highly variable sites. These also were distributed randomly. Thus hypervariability, which has been observed in all other serine proteinase inhibitor families to date, appears to be lacking in the proteinase inhibitor I family. |
| abstractGer |
Abstract A protein phylogenetic tree was constructed from 24 homologous proteinase inhibitor I sequences identified in the EMBUGenbank and Swiss-Prot databases and from translated amino acid data from four constitutive cDNA clones of proteinase inhibitor I characterized from potato tuber mRNA. The tree suggests that divergence of at least four paralogous proteins with functional specialization occurred at different times during the evolutionary history of the proteinase inhibitor I family. Five distinct regions in the primary structure, earlier identified by structural studies, were used to analyze the inhibitor family for hypervariability (Creighton and Darby, Trends Biochem Sci 14:319–324, 1989). Mutations did not occur with higher-than-random frequency within the proteinase binding region. When isoinhibitor, orthologous, or paralogous data subsets were subsequently analyzed the same results were obtained. Comparison of the amino acid sequences for all the known potato proteinase isoinhibitor I proteins identified ten highly variable sites. These also were distributed randomly. Thus hypervariability, which has been observed in all other serine proteinase inhibitor families to date, appears to be lacking in the proteinase inhibitor I family. |
| abstract_unstemmed |
Abstract A protein phylogenetic tree was constructed from 24 homologous proteinase inhibitor I sequences identified in the EMBUGenbank and Swiss-Prot databases and from translated amino acid data from four constitutive cDNA clones of proteinase inhibitor I characterized from potato tuber mRNA. The tree suggests that divergence of at least four paralogous proteins with functional specialization occurred at different times during the evolutionary history of the proteinase inhibitor I family. Five distinct regions in the primary structure, earlier identified by structural studies, were used to analyze the inhibitor family for hypervariability (Creighton and Darby, Trends Biochem Sci 14:319–324, 1989). Mutations did not occur with higher-than-random frequency within the proteinase binding region. When isoinhibitor, orthologous, or paralogous data subsets were subsequently analyzed the same results were obtained. Comparison of the amino acid sequences for all the known potato proteinase isoinhibitor I proteins identified ten highly variable sites. These also were distributed randomly. Thus hypervariability, which has been observed in all other serine proteinase inhibitor families to date, appears to be lacking in the proteinase inhibitor I family. |
| collection_details |
GBV_USEFLAG_U ZDB-1-SOJ GBV_NL_ARTICLE |
| title_short |
Evolution of the proteinase inhibitor I family and apparent lack of hypervariability in the proteinase contact loop |
| url |
http://dx.doi.org/10.1007/BF00160410 |
| remote_bool |
true |
| author2 |
Beuning, Lesley L. Spriggs, Thomas W. Christeller, John T. |
| author2Str |
Beuning, Lesley L. Spriggs, Thomas W. Christeller, John T. |
| ppnlink |
NLEJ188994645 |
| mediatype_str_mv |
z |
| isOA_txt |
false |
| hochschulschrift_bool |
false |
| author2_role |
oth oth oth |
| up_date |
2024-07-06T08:44:36.014Z |
| _version_ |
1803818606017904640 |
| fullrecord_marcxml |
<?xml version="1.0" encoding="UTF-8"?><collection xmlns="http://www.loc.gov/MARC21/slim"><record><leader>01000caa a22002652 4500</leader><controlfield tag="001">NLEJ20710042X</controlfield><controlfield tag="003">DE-627</controlfield><controlfield tag="005">20210706221051.0</controlfield><controlfield tag="007">cr uuu---uuuuu</controlfield><controlfield tag="008">070528s1994 xx |||||o 00| ||eng c</controlfield><datafield tag="035" ind1=" " ind2=" "><subfield code="a">(DE-627)NLEJ20710042X</subfield></datafield><datafield tag="040" ind1=" " ind2=" "><subfield code="a">DE-627</subfield><subfield code="b">ger</subfield><subfield code="c">DE-627</subfield><subfield code="e">rakwb</subfield></datafield><datafield tag="041" ind1=" " ind2=" "><subfield code="a">eng</subfield></datafield><datafield tag="245" ind1="1" ind2="0"><subfield code="a">Evolution of the proteinase inhibitor I family and apparent lack of hypervariability in the proteinase contact loop</subfield></datafield><datafield tag="264" ind1=" " ind2="1"><subfield code="c">1994</subfield></datafield><datafield tag="300" ind1=" " ind2=" "><subfield code="a">11</subfield></datafield><datafield tag="336" ind1=" " ind2=" "><subfield code="a">nicht spezifiziert</subfield><subfield code="b">zzz</subfield><subfield code="2">rdacontent</subfield></datafield><datafield tag="337" ind1=" " ind2=" "><subfield code="a">nicht spezifiziert</subfield><subfield code="b">z</subfield><subfield code="2">rdamedia</subfield></datafield><datafield tag="338" ind1=" " ind2=" "><subfield code="a">nicht spezifiziert</subfield><subfield code="b">zu</subfield><subfield code="2">rdacarrier</subfield></datafield><datafield tag="520" ind1=" " ind2=" "><subfield code="a">Abstract A protein phylogenetic tree was constructed from 24 homologous proteinase inhibitor I sequences identified in the EMBUGenbank and Swiss-Prot databases and from translated amino acid data from four constitutive cDNA clones of proteinase inhibitor I characterized from potato tuber mRNA. The tree suggests that divergence of at least four paralogous proteins with functional specialization occurred at different times during the evolutionary history of the proteinase inhibitor I family. Five distinct regions in the primary structure, earlier identified by structural studies, were used to analyze the inhibitor family for hypervariability (Creighton and Darby, Trends Biochem Sci 14:319–324, 1989). Mutations did not occur with higher-than-random frequency within the proteinase binding region. When isoinhibitor, orthologous, or paralogous data subsets were subsequently analyzed the same results were obtained. Comparison of the amino acid sequences for all the known potato proteinase isoinhibitor I proteins identified ten highly variable sites. These also were distributed randomly. Thus hypervariability, which has been observed in all other serine proteinase inhibitor families to date, appears to be lacking in the proteinase inhibitor I family.</subfield></datafield><datafield tag="533" ind1=" " ind2=" "><subfield code="f">Springer Online Journal Archives 1860-2002</subfield></datafield><datafield tag="700" ind1="1" ind2=" "><subfield code="a">Beuning, Lesley L.</subfield><subfield code="4">oth</subfield></datafield><datafield tag="700" ind1="1" ind2=" "><subfield code="a">Spriggs, Thomas W.</subfield><subfield code="4">oth</subfield></datafield><datafield tag="700" ind1="1" ind2=" "><subfield code="a">Christeller, John T.</subfield><subfield code="4">oth</subfield></datafield><datafield tag="773" ind1="0" ind2="8"><subfield code="i">in</subfield><subfield code="t">Journal of molecular evolution</subfield><subfield code="d">1971</subfield><subfield code="g">39(1994) vom: Juni, Seite 644-654</subfield><subfield code="w">(DE-627)NLEJ188994645</subfield><subfield code="w">(DE-600)1464309-1</subfield><subfield code="x">1432-1432</subfield><subfield code="7">nnns</subfield></datafield><datafield tag="773" ind1="1" ind2="8"><subfield code="g">volume:39</subfield><subfield code="g">year:1994</subfield><subfield code="g">month:06</subfield><subfield code="g">pages:644-654</subfield><subfield code="g">extent:11</subfield></datafield><datafield tag="856" ind1="4" ind2="0"><subfield code="u">http://dx.doi.org/10.1007/BF00160410</subfield></datafield><datafield tag="912" ind1=" " ind2=" "><subfield code="a">GBV_USEFLAG_U</subfield></datafield><datafield tag="912" ind1=" " ind2=" "><subfield code="a">ZDB-1-SOJ</subfield></datafield><datafield tag="912" ind1=" " ind2=" "><subfield code="a">GBV_NL_ARTICLE</subfield></datafield><datafield tag="951" ind1=" " ind2=" "><subfield code="a">AR</subfield></datafield><datafield tag="952" ind1=" " ind2=" "><subfield code="d">39</subfield><subfield code="j">1994</subfield><subfield code="c">6</subfield><subfield code="h">644-654</subfield><subfield code="g">11</subfield></datafield></record></collection>
|
| score |
7.400407 |