Dataset Information

Isolation and developmental expression of a rat cDNA encoding a cysteine-rich zinc finger protein.

ABSTRACT: A number of cysteine-rich proteins have recently been isolated by homology screening, differential library screens, and association with other proteins. In this report, we describe the isolation of the rat cysteine-rich protein from a rat brain library during a search for clones with homology to the delta-opioid receptor. One of the cDNAs isolated hybridized to a 1.8 kb mRNA abundantly expressed throughout the rat brain as well as in rat liver. In situ hybridization reveals a wide distribution in rat brain; in particular, abundant hybridization was detected in the hippocampus, cerebellum, habenula, reticular thalamic nucleus and interposed nucleus. Nucleotide sequence analysis of a 1403 bp cDNA clone indicated 77% identity with the cDNA for human cysteine-rich protein (hCRP), that translates into a 99% identity at the amino acid level. The predicted amino acid sequence suggests four zinc fingers, two of the C4 class and two of the C2HC class. This structural motif is characteristic of members of the LIM domain protein family. The mRNA is serum-inducible in Balb/c 3T3 cells. Additional study suggests that its expression is not induced by either NGF treatment of PC12h pheochromocytoma cells, or inflammation-induced injury in the spinal cord at up to 60 min after injury. It does appear to be developmentally expressed in rat brain, consistent with a potential role in neuronal development. The rat CRP clone will be useful for studying the function of CRPs in rodent models.

SUBMITTER: McLaughlin CR

PROVIDER: S-EPMC332101 | biostudies-other | 1994 Dec

REPOSITORIES: biostudies-other

ACCESS DATA

Publications

Isolation and developmental expression of a rat cDNA encoding a cysteine-rich zinc finger protein.

McLaughlin C R CR Tao Q Q Abood M E ME

Nucleic acids research 19941201 24

A number of cysteine-rich proteins have recently been isolated by homology screening, differential library screens, and association with other proteins. In this report, we describe the isolation of the rat cysteine-rich protein from a rat brain library during a search for clones with homology to the delta-opioid receptor. One of the cDNAs isolated hybridized to a 1.8 kb mRNA abundantly expressed throughout the rat brain as well as in rat liver. In situ hybridization reveals a wide distribution i ...[more]

PMID: 7816640

Similar Datasets

Project description:BackgroundTransposons are mobile genetic elements that colonize genomes and drive their plasticity in all organisms. DNA transposon-encoded transposases bind to the ends of their cognate transposons and catalyze their movement. In some cases, exaptation of transposon genes has allowed novel cellular functions to emerge. The PiggyMac (Pgm) endonuclease of the ciliate Paramecium tetraurelia is a domesticated transposase from the PiggyBac family. It carries a core catalytic domain typical of PiggyBac-related transposases and a short cysteine-rich domain (CRD), flanked by N- and C-terminal extensions. During sexual processes Pgm catalyzes programmed genome rearrangements (PGR) that eliminate ~ 30% of germline DNA from the somatic genome at each generation. How Pgm recognizes its DNA cleavage sites in chromatin is unclear and the structure-function relationships of its different domains have remained elusive.ResultsWe provide insight into Pgm structure by determining the fold adopted by its CRD, an essential domain required for PGR. Using Nuclear Magnetic Resonance, we show that the Pgm CRD binds two Zn2+ ions and forms an unusual binuclear cross-brace zinc finger, with a circularly permutated treble-clef fold flanked by two flexible arms. The Pgm CRD structure clearly differs from that of several other PiggyBac-related transposases, among which is the well-studied PB transposase from Trichoplusia ni. Instead, the arrangement of cysteines and histidines in the primary sequence of the Pgm CRD resembles that of active transposases from piggyBac-like elements found in other species and of human PiggyBac-derived domesticated transposases. We show that, unlike the PB CRD, the Pgm CRD does not bind DNA. Instead, it interacts weakly with the N-terminus of histone H3, whatever its lysine methylation state.ConclusionsThe present study points to the structural diversity of the CRD among transposases from the PiggyBac family and their domesticated derivatives, and highlights the diverse interactions this domain may establish with chromatin, from sequence-specific DNA binding to contacts with histone tails. Our data suggest that the Pgm CRD fold, whose unusual arrangement of cysteines and histidines is found in all PiggyBac-related domesticated transposases from Paramecium and Tetrahymena, was already present in the ancestral active transposase that gave rise to ciliate domesticated proteins.

Dataset Information

Isolation and developmental expression of a rat cDNA encoding a cysteine-rich zinc finger protein.

Publications

Isolation and developmental expression of a rat cDNA encoding a cysteine-rich zinc finger protein.

Similar Datasets

OmicsDI is part of the ELIXIR infrastructure