Gene/Protein Disease Symptom Drug Enzyme Compound
Pivot Concepts:   Target Concepts:
Query: EC:3.1.31.1 (micrococcal nuclease)
 2,818 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

A comprehensive review of the methods which have been utilized for the identification of staphylococci is presented. Biochemical characteristics which have assisted in the primary isolation of staphylococci, such as pigmentation, hemolytic activity, the egg yolk phenomenon, and deoxyribonuclease and coagulase production, are also analyzed. The potential applicability of advanced techniques to identify staphylococci, such as the detection of enterotoxin production, base ratio analysis, cell wall analysis, phage typing, and serology, is discussed. The following procedures are recommended for routine use: Idnetification of Staphylococcus sp. (clinical laboratories): microscopic observation, catalase activity, coagulase production, lysostaphin sensitivity, and (optional) facultative growth in thioglycolate medium. Identification of Staphylococcus aureus (food laboratories): microscopic observation, catalase activity, coagulase production, thermonuclease production, and (optional) lysostaphin sensitivity.
CRC Crit Rev Clin Lab Sci 1976
PMID:The identification of staphylococci in clinical and food microbiology laboratories. 79 25

Transcriptionally active or potentially active genes can be distinguished by several criteria from inactive sequences. Active genes show both an increased general sensitivity to endonucleases like DNase I or micrococcal nuclease and the presence of nuclease hypersensitive sites. Frequently, the nuclease hypersensitive sites are present just upstream of the transcription initiation site covering sequences that are crucial for the promoter function. Viral or cellular transcription enhancer elements are also associated with DNase I hypersensitive sites. At least for the SV40 enhancer, it was shown by electronmicroscopic studies that the DNase I hypersensitive DNA segment is excluded from nucleosomes. It is highly plausible that the binding of regulatory proteins to enhancer or promoter sequences is responsible for the exclusion of these DNA segments from nucleosomes and for the formation of nuclease hypersensitive sites. We speculate that the binding of such proteins may switch on a change in the conformation and/or the protein composition of a chromatin segment or domain containing one to several genes. Biochemical analysis of fractionated nucleosome particles or of active and inactive chromatin fractions have revealed differences in the composition as well as in the degree of modification of histones in these two subfractions of the chromosome. However, until present it is impossible to define unambiguously what are the crucial structural elements that distinguish between particles present on active and inactive chromatin.
CRC Crit Rev Biochem 1986
PMID:Structure of transcriptionally active chromatin. 301 90