A novel nucleic acid-binding protein in the cyanobacterium Synechococcus sp. PCC6301: a soluble 33-kDa polypeptide with high sequence similarity to ribosomal protein S1

被引：0

作者：

C. Sugita

M. Sugiura

M. Sugita

机构：

[1] Center for Gene Research,

[2] Graduate School of Human Informatics,undefined

[3] Nagoya University,undefined

[4] Nagoya 464-8601,undefined

[5] Japan E-mail: sugita@info.human.nagoya-u.ac.jp Tel./Fax: +81-52-789-4779,undefined

来源：

Molecular and General Genetics MGG | 2000年 / 263卷

关键词：

Key words Cyanobacteria; Ribosomal protein S1; Nucleic acid-binding protein; S1 motif; Ribosome;

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摘要：

Cyanobacteria are prokaryotes that carry out plant-type photosynthesis and contain several eukaryotic-type RNA-binding proteins. Using a single-stranded DNA column, a 33-kDa protein was isolated and characterized from Synechococcus sp. PCC6301. This protein of 293 amino acids is similar in overall structure to the ribosomal protein S1 found in the same species, and contains three repeated units that are highly similar to the S1 motif originally found in the ribosomal protein S1 of Escherichia coli. However, the 33-kDa protein was found not to be associated with ribosomes and its nucleic acid binding specificity is distinct from that of the ribosomal protein S1. As this protein has high affinity for both single- and double-stranded DNA, as well as for poly(G) and poly(A), we tentatively named it nucleic acid-binding protein 1 (Nbp1).

引用

页码：655 / 663

页数：8