The histone-like H protein ofEscherichia coliis ribosomal protein S3
نویسندگان
چکیده
منابع مشابه
The histone-like H protein of Escherichia coli is ribosomal protein S3.
We report the purification of four proteins from Escherichia coli that stimulate or inhibit inter- and/or intramolecular recombination promoted by the yeast plasmid-encoded FLP protein. The proteins are identified as the ribosomal proteins S3 (27 kDa), L2 (26 kDa), S4 (24 kDa), and S5 (16 kDa), on the basis of N-terminal sequence analysis. The S3 protein is found to be identical to H protein, a...
متن کاملThe primary structure of rat ribosomal protein S3.
The amino acid sequence of rat ribosomal protein S3, which has been reported to form part of the binding site for initiation factors, was deduced from the sequence of nucleotides in a recombinant cDNA. Ribosomal protein S3 contains 243 amino acids and has a molecular weight of 26,643. Rat S3 and Xenopus laevis ribosomal protein S1 are homologous: There are 62 identities in 63 consecutive residu...
متن کاملIsolation of a cDNA encoding human 40S ribosomal protein s3.
A cDNA which encodes human 40S ribosomal protein s3 has been isolated from a lambda-Gem 2 cDNA library constructed using poly (A+) RNA from human WISH cells. The cDNA insert includes a 5' noncoding sequence of 22 nucleotides, an open reading frame of 729 nucleotides and a 3' noncoding sequence of 82 nucleotides followed by a 3' poly A tail. The hexameter AATAAA, which is the signal sequence for...
متن کاملThe T4 phage DNA mimic protein Arn inhibits the DNA binding activity of the bacterial histone-like protein H-NS.
The T4 phage protein Arn (Anti restriction nuclease) was identified as an inhibitor of the restriction enzyme McrBC. However, until now its molecular mechanism remained unclear. In the present study we used structural approaches to investigate biological properties of Arn. A structural analysis of Arn revealed that its shape and negative charge distribution are similar to dsDNA, suggesting that...
متن کاملHistone-like protein of Streptomyces lividans
A DNA-bineting protein (about lOkDa and pI>9.7) of Streptomyces lividans TK24 was purified on a denatured DNA-Cellulose column, and then on a native DNA-Cellulose column. The N-terminal amino acid sequence of this protein had high homology with those of small basic DNA-binding proteins known as histone-like proteins. Thus, this protein was designated HSI (histone-like protein of ::J.. lividans)...
متن کاملذخیره در منابع من
با ذخیره ی این منبع در منابع من، دسترسی به آن را برای استفاده های بعدی آسان تر کنید
ژورنال
عنوان ژورنال: Nucleic Acids Research
سال: 1989
ISSN: 0305-1048,1362-4962
DOI: 10.1093/nar/17.8.3145