Role of the ribosome-associated protein PY in the cold-shock response of Escherichia coli

被引:16
|
作者
Di Pietro, Fabio [1 ]
Brandi, Anna [1 ]
Dzeladini, Nadire [1 ]
Fabbretti, Attilio [1 ]
Carzaniga, Thomas [2 ]
Piersimoni, Lolita [3 ]
Pon, Cynthia L. [1 ]
Giuliodori, Anna Maria [1 ]
机构
[1] Univ Camerino, Sch Biosci & Biotechnol, Lab Mol Biol & Biotechnol, I-62032 Camerino, MC, Italy
[2] Univ Milan, Dipartimento Biosci, I-20133 Milan, Italy
[3] Univ Michigan, Dept Mol Cellular & Dev Biol, Ann Arbor, MI 48109 USA
来源
MICROBIOLOGYOPEN | 2013年 / 2卷 / 02期
关键词
Cold shock; protein PY; translation initiation; translation regulation; TRANSLATION INITIATION; CSPA FAMILY; GEL-ELECTROPHORESIS; MESSENGER-RNAS; BINDING FACTOR; EXPRESSION; SUBUNIT; GENE; IDENTIFICATION; PURIFICATION;
D O I
10.1002/mbo3.68
中图分类号
Q93 [微生物学];
学科分类号
071005 ; 100705 ;
摘要
Protein Y (PY) is an Escherichia coli cold-shock protein which has been proposed to be responsible for the repression of bulk protein synthesis during cold adaptation. Here, we present in vivo and in vitro data which clarify the role of PY and its mechanism of action. Deletion of yfiA, the gene encoding protein PY, demonstrates that this protein is dispensable for cold adaptation and is not responsible for the shutdown of bulk protein synthesis at the onset of the stress, although it is able to partially inhibit translation. In vitro assays reveal that the extent of PY inhibition changes with different mRNAs and that this inhibition is related to the capacity of PY of binding 30S subunits with a fairly strong association constant, thus stimulating the formation of 70S monomers. Furthermore, our data provide evidence that PY competes with the other ribosomal ligands for the binding to the 30S subunits. Overall these results suggest an alternative model to explain PY function during cold shock and to reconcile the inhibition caused by PY with the active translation observed for some mRNAs during cold shock.
引用
收藏
页码:293 / 307
页数:15
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