Gene/Protein Disease Symptom Drug Enzyme Compound
Pivot Concepts:   Target Concepts:
Query: EC:3.4.24.3 (collagenase)
 18,340 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

The ETS transcription factor family is characterized by a conserved ETS DNA-binding domain and its members have been implicated in a plethora of biological processes, including development, cell transformation and metastasis. ER71 is a testis-specific ETS protein that is not homologous to any other protein outside its ETS domain, suggesting that it fulfills a unique physiological role. Here, we report that ER71 is a constitutively nuclear protein whose intracellular localization is dependent on a portion of the ETS domain, namely ER71 amino acids 276-315. Furthermore, the DNA binding activity is intramolecularly regulated, as the N-terminus of ER71 has a negative effect on DNA binding while the C-terminus dramatically enhances this activity. We also demonstrate that ER71 possesses an extremely potent N-terminal transactivation domain comprised of amino acids 1-157. Finally, we show that ER71 is capable of directly activating both an E74 site-driven and the matrix metalloproteinase-1 promoter. Altogether, these data represent the first functional characterization of ER71, which may perform important functions in the developing and adult testis as well as in testicular germ cell tumorigenesis.
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PMID:Functional analysis of the transcription factor ER71 and its activation of the matrix metalloproteinase-1 promoter. 1208 83

Testis-specific gene A (TSGA) was originally identified in rat and shown to be expressed within the testes. Here, we have cloned the murine homolog [also known as jumonji domain-containing 1a (Jmjd1a)] and for the first time characterized the TSGA protein and its functions. Although murine TSGA is expressed in testes, its mRNA is also present in many other tissues, including heart, thymus, liver, and skin. Immunostaining revealed that TSGA is a nuclear protein, whose N-terminus contains a putative nuclear localization signal. TSGA displays significant homology to a suspected tumor suppressor and coactivator (5qNCA), to a thyroid hormone receptor interacting protein (TRIP8) and to the corepressor Hairless, pointing at a role of TSGA in transcription regulation. Indeed, TSGA contains several functional transcription repression domains. In addition, TSGA interacts both in vitro and in vivo with ER71 (ETS related 71), a transcription factor that is expressed in the testes of adult mice and during embryogenesis. Specifically, the N-terminus of TSGA and the C-terminus of ER71 are primarily engaged in their complex formation. Furthermore, TSGA impairs the ability of ER71 to activate transcription from the matrix metalloproteinase-1 promoter. Thus, TSGA may modulate the function of ER71 and thereby affect spermatogenesis as well as embryonic development.
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PMID:Repression of transcription by TSGA/Jmjd1a, a novel interaction partner of the ETS protein ER71. 1661 73