Preferential conservation of the globular domains of the βA3/A1-crystallin polypeptide of the chicken eye lens

Charlotte A. Peterson; Joram Piatigorsky

doi:10.1016/0378-1119(86)90248-9

Preferential conservation of the globular domains of the βA3/A1-crystallin polypeptide of the chicken eye lens

Charlotte A. Peterson
, Joram Piatigorsky

Physical Therapy

Research output: Contribution to journal › Article › peer-review

45 Scopus citations

Abstract

The primary structure of the β19/26-cry stallin polypeptide of the chicken lens has been determined by cDNA sequencing and primer extension experiments. In addition, a primer extension experiment has corrected the sequence for the N-terminal arm of the murine β23 polypeptide, which is the homologue of the chicken β19/26 polypeptide.We also show that, in the chicken and mouse, the N-terminal arm of the polypeptide is encoded on two separate exons. For simplicity, we have changed the names of both chicken β19/26 and murine β23 to βA3/A1,which is the name of the homologous bovine polypeptide. The deduced sequence of the chicken βA3/A1 polypeptide fits the predicted three-dimensional structure involving two homologous domains, each folded into two 'Greek key' motifs,common to the βγ-crystallin superfamily of proteins. Comparison of the amino acid sequence of the chicken and mammalian βA3/A1 polypeptides indicates that different regions of the protein, which are encoded on different exons, are diverging at different rates.The N-terminal extension is the fastest evolving region of the βA3/A1 polypeptide. Hybrid-selected translation coupled with primer extension experiments suggest that a single chicken βA3/A1 mRNA synthesizes two polypeptides, βA3 (25 kDa) and βA1(23 kDa) by utilization of different translation initiation sites.

Original language	English
Pages (from-to)	139-147
Number of pages	9
Journal	Gene
Volume	45
Issue number	2
DOIs	https://doi.org/10.1016/0378-1119(86)90248-9
State	Published - 1986

Bibliographical note

Funding Information:
We are gratefult o Dr. Mark A. Thompson for continuala dvicea nd interestin this work. We also thankD r. J. FieldingH ejtmancikf or the freeu seo f thec DNA clonesh ep reparedin our laboratoryD, rs. PeterC ollins,M elanieS pringsa, ndA na Chepelinsky for advice on primer extensione xperimentsD, r. GraemeJ . Wistowf or helpfuld iscussionos n protein structurea nd Mrs. Dawn Chicchirichi for expert typingo f this manuscriptC. AP is supportedb y NIH post-doctoragl rant5F32-EY05816-02.

Funding

We are gratefult o Dr. Mark A. Thompson for continuala dvicea nd interestin this work. We also thankD r. J. FieldingH ejtmancikf or the freeu seo f thec DNA clonesh ep reparedin our laboratoryD, rs. PeterC ollins,M elanieS pringsa, ndA na Chepelinsky for advice on primer extensione xperimentsD, r. GraemeJ . Wistowf or helpfuld iscussionos n protein structurea nd Mrs. Dawn Chicchirichi for expert typingo f this manuscriptC. AP is supportedb y NIH post-doctoragl rant5F32-EY05816-02.

Funders	Funder number
NIH post-doctoragl rant5F32-EY05816-02	rant5F32-EY05816-02
National Eye Institute (NEI)	F32EY005816

Keywords

'Greek key' motifs
Recombinant DNA
bovine
cDNA sequencing
exons
molecular evolution
murine
primer extension

ASJC Scopus subject areas

Genetics

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10.1016/0378-1119(86)90248-9

Cite this

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title = "Preferential conservation of the globular domains of the βA3/A1-crystallin polypeptide of the chicken eye lens",

abstract = "The primary structure of the β19/26-cry stallin polypeptide of the chicken lens has been determined by cDNA sequencing and primer extension experiments. In addition, a primer extension experiment has corrected the sequence for the N-terminal arm of the murine β23 polypeptide, which is the homologue of the chicken β19/26 polypeptide.We also show that, in the chicken and mouse, the N-terminal arm of the polypeptide is encoded on two separate exons. For simplicity, we have changed the names of both chicken β19/26 and murine β23 to βA3/A1,which is the name of the homologous bovine polypeptide. The deduced sequence of the chicken βA3/A1 polypeptide fits the predicted three-dimensional structure involving two homologous domains, each folded into two 'Greek key' motifs,common to the βγ-crystallin superfamily of proteins. Comparison of the amino acid sequence of the chicken and mammalian βA3/A1 polypeptides indicates that different regions of the protein, which are encoded on different exons, are diverging at different rates.The N-terminal extension is the fastest evolving region of the βA3/A1 polypeptide. Hybrid-selected translation coupled with primer extension experiments suggest that a single chicken βA3/A1 mRNA synthesizes two polypeptides, βA3 (25 kDa) and βA1(23 kDa) by utilization of different translation initiation sites.",

keywords = "'Greek key' motifs, Recombinant DNA, bovine, cDNA sequencing, exons, molecular evolution, murine, primer extension",

author = "Peterson, \{Charlotte A.\} and Joram Piatigorsky",

note = "Funding Information: We are gratefult o Dr. Mark A. Thompson for continuala dvicea nd interestin this work. We also thankD r. J. FieldingH ejtmancikf or the freeu seo f thec DNA clonesh ep reparedin our laboratoryD, rs. PeterC ollins,M elanieS pringsa, ndA na Chepelinsky for advice on primer extensione xperimentsD, r. GraemeJ . Wistowf or helpfuld iscussionos n protein structurea nd Mrs. Dawn Chicchirichi for expert typingo f this manuscriptC. AP is supportedb y NIH post-doctoragl rant5F32-EY05816-02.",

year = "1986",

doi = "10.1016/0378-1119(86)90248-9",

language = "English",

volume = "45",

pages = "139--147",

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TY - JOUR

T1 - Preferential conservation of the globular domains of the βA3/A1-crystallin polypeptide of the chicken eye lens

AU - Peterson, Charlotte A.

AU - Piatigorsky, Joram

N1 - Funding Information: We are gratefult o Dr. Mark A. Thompson for continuala dvicea nd interestin this work. We also thankD r. J. FieldingH ejtmancikf or the freeu seo f thec DNA clonesh ep reparedin our laboratoryD, rs. PeterC ollins,M elanieS pringsa, ndA na Chepelinsky for advice on primer extensione xperimentsD, r. GraemeJ . Wistowf or helpfuld iscussionos n protein structurea nd Mrs. Dawn Chicchirichi for expert typingo f this manuscriptC. AP is supportedb y NIH post-doctoragl rant5F32-EY05816-02.

PY - 1986

Y1 - 1986

N2 - The primary structure of the β19/26-cry stallin polypeptide of the chicken lens has been determined by cDNA sequencing and primer extension experiments. In addition, a primer extension experiment has corrected the sequence for the N-terminal arm of the murine β23 polypeptide, which is the homologue of the chicken β19/26 polypeptide.We also show that, in the chicken and mouse, the N-terminal arm of the polypeptide is encoded on two separate exons. For simplicity, we have changed the names of both chicken β19/26 and murine β23 to βA3/A1,which is the name of the homologous bovine polypeptide. The deduced sequence of the chicken βA3/A1 polypeptide fits the predicted three-dimensional structure involving two homologous domains, each folded into two 'Greek key' motifs,common to the βγ-crystallin superfamily of proteins. Comparison of the amino acid sequence of the chicken and mammalian βA3/A1 polypeptides indicates that different regions of the protein, which are encoded on different exons, are diverging at different rates.The N-terminal extension is the fastest evolving region of the βA3/A1 polypeptide. Hybrid-selected translation coupled with primer extension experiments suggest that a single chicken βA3/A1 mRNA synthesizes two polypeptides, βA3 (25 kDa) and βA1(23 kDa) by utilization of different translation initiation sites.

AB - The primary structure of the β19/26-cry stallin polypeptide of the chicken lens has been determined by cDNA sequencing and primer extension experiments. In addition, a primer extension experiment has corrected the sequence for the N-terminal arm of the murine β23 polypeptide, which is the homologue of the chicken β19/26 polypeptide.We also show that, in the chicken and mouse, the N-terminal arm of the polypeptide is encoded on two separate exons. For simplicity, we have changed the names of both chicken β19/26 and murine β23 to βA3/A1,which is the name of the homologous bovine polypeptide. The deduced sequence of the chicken βA3/A1 polypeptide fits the predicted three-dimensional structure involving two homologous domains, each folded into two 'Greek key' motifs,common to the βγ-crystallin superfamily of proteins. Comparison of the amino acid sequence of the chicken and mammalian βA3/A1 polypeptides indicates that different regions of the protein, which are encoded on different exons, are diverging at different rates.The N-terminal extension is the fastest evolving region of the βA3/A1 polypeptide. Hybrid-selected translation coupled with primer extension experiments suggest that a single chicken βA3/A1 mRNA synthesizes two polypeptides, βA3 (25 kDa) and βA1(23 kDa) by utilization of different translation initiation sites.

KW - 'Greek key' motifs

KW - Recombinant DNA

KW - bovine

KW - cDNA sequencing

KW - exons

KW - molecular evolution

KW - murine

KW - primer extension

UR - https://www.scopus.com/pages/publications/0023029875

UR - https://www.scopus.com/pages/publications/0023029875#tab=citedBy

U2 - 10.1016/0378-1119(86)90248-9

DO - 10.1016/0378-1119(86)90248-9

M3 - Article

C2 - 3803920

AN - SCOPUS:0023029875

SN - 0378-1119

VL - 45

SP - 139

EP - 147

JO - Gene

JF - Gene

IS - 2

ER -

Preferential conservation of the globular domains of the βA3/A1-crystallin polypeptide of the chicken eye lens

Abstract

Bibliographical note

Funding

Keywords

ASJC Scopus subject areas

Access to Document

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