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Sequence and organization of the mouse poly (ADP-ribose) polymerase gene.

ABSTRACT: Using a human cDNA probe, we have isolated murine genomic and cDNA clones corresponding to the nuclear enzyme poly (ADP-ribose) polymerase (ADPRP). Northern analysis with the mouse cDNA clones reveals transcripts of 3.7-3.8 kb corresponding in size to the human ADPRP transcript. DNA sequence comparisons between mouse and human clones reveals extensive amino acid sequence conservation within regions harboring DNA binding, NAD+ binding or automodification domains. A survey among mouse inbred strains for restriction fragment length polymorphism (RFLP) reveals at least three distinct ADPRP alleles. The segregation of alleles among mouse genetic recombinants positions ADPRP on mouse chromosome 1 between the complement receptor-related gene At-3 and the Fc receptor locus FcR. Furthermore, ADPRP is closely associated with the autoimmune locus gld (generalized lymphadenopathy).

SUBMITTER: Huppi K

PROVIDER: S-EPMC317782 | biostudies-other | 1989 May

REPOSITORIES: biostudies-other

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Sequence and organization of the mouse poly (ADP-ribose) polymerase gene.

Huppi K K Bhatia K K Siwarski D D Klinman D D Cherney B B Smulson M M

Nucleic acids research 19890501 9

Using a human cDNA probe, we have isolated murine genomic and cDNA clones corresponding to the nuclear enzyme poly (ADP-ribose) polymerase (ADPRP). Northern analysis with the mouse cDNA clones reveals transcripts of 3.7-3.8 kb corresponding in size to the human ADPRP transcript. DNA sequence comparisons between mouse and human clones reveals extensive amino acid sequence conservation within regions harboring DNA binding, NAD+ binding or automodification domains. A survey among mouse inbred strai ...[more]

PMID: 2498841

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Project description:The poly(ADP-ribose) polymerase (PARP) superfamily was originally identified as enzymes that catalyze the attachment of ADP-ribose subunits to target proteins using NAD+ as a substrate. The family is characterized by the catalytic site, termed the PARP signature. While these proteins can be found in a range of eukaryotes, they have been best studied in mammals. In these organisms, PARPs have key functions in DNA repair, genome integrity and epigenetic regulation. More recently it has been found that proteins within the PARP superfamily have altered catalytic sites, and have mono(ADP-ribose) transferase (mART) activity or are enzymatically inactive. These findings suggest that the PARP signature has a broader range of functions that initially predicted. In this study, we investigate the evolutionary history of PARP genes across the eukaryotes.We identified in silico 236 PARP proteins from 77 species across five of the six eukaryotic supergroups. We performed extensive phylogenetic analyses of the identified PARPs. They are found in all eukaryotic supergroups for which sequence is available, but some individual lineages within supergroups have independently lost these genes. The PARP superfamily can be subdivided into six clades. Two of these clades were likely found in the last common eukaryotic ancestor. In addition, we have identified PARPs in organisms in which they have not previously been described.Three main conclusions can be drawn from our study. First, the broad distribution and pattern of representation of PARP genes indicates that the ancestor of all extant eukaryotes encoded proteins of this type. Second, the ancestral PARP proteins had different functions and activities. One of these proteins was similar to human PARP1 and likely functioned in DNA damage response. The second of the ancestral PARPs had already evolved differences in its catalytic domain that suggest that these proteins may not have possessed poly(ADP-ribosyl)ation activity. Third, the diversity of the PARP superfamily is larger than previously documented, suggesting as more eukaryotic genomes become available, this gene family will grow in both number and type.

Dataset Information

Sequence and organization of the mouse poly (ADP-ribose) polymerase gene.

Publications

Sequence and organization of the mouse poly (ADP-ribose) polymerase gene.

Similar Datasets

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