MMS19 Assembles Iron-Sulfur Proteins Required for DNA Metabolism and Genomic Integrity

被引：219

作者：

Stehling, Oliver ^{[2
,3
]}

Vashisht, Ajay A. ^{[1
]}

Mascarenhas, Judita ^{[2
,3
]}

Jonsson, Zophonias O. ^{[1
]}

Sharma, Tanu ^{[1
]}

Netz, Daili J. A. ^{[2
,3
]}

Pierik, Antonio J. ^{[2
,3
]}

Wohlschlegel, James A. ^{[1
]}

Lill, Roland ^{[2
,3
]}

机构：

[1] Univ Calif Los Angeles, David Geffen Sch Med, Dept Biol Chem, Los Angeles, CA 90095 USA

[2] Univ Marburg, Inst Zytobiol & Zytopathol, D-35033 Marburg, Germany

[3] Max Planck Inst Terr Mikrobiol, D-35043 Marburg, Germany

来源：

SCIENCE | 2012年 / 337卷 / 6091期

关键词：

NUCLEOTIDE EXCISION-REPAIR; SACCHAROMYCES-CEREVISIAE; CLUSTER; DAMAGE; HOMEOSTASIS; BIOGENESIS; TFIIH; INSTABILITY; MATURATION; HELICASES;

D O I：

10.1126/science.1219723

中图分类号：

O [数理科学和化学]; P [天文学、地球科学]; Q [生物科学]; N [自然科学总论];

学科分类号：

07 ; 0710 ; 09 ;

摘要：

Instability of the nuclear genome is a hallmark of cancer and aging. MMS19 protein has been linked to maintenance of genomic integrity, but the molecular basis of this connection is unknown. Here, we identify MMS19 as a member of the cytosolic iron-sulfur protein assembly (CIA) machinery. MMS19 functions as part of the CIA targeting complex that specifically interacts with and facilitates iron-sulfur cluster insertion into apoproteins involved in methionine biosynthesis, DNA replication, DNA repair, and telomere maintenance. MMS19 thus serves as an adapter between early-acting CIA components and a subset of cellular iron-sulfur proteins. The function of MMS19 in the maturation of crucial components of DNA metabolism may explain the sensitivity of MMS19 mutants to DNA damage and the presence of extended telomeres.

引用

页码：195 / 199

页数：5

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