Structure and degradation mechanisms of 3′ to 5′ exoribonucleases

Research output: Chapter in Book/Report/Conference proceedingChapter

Abstract

Exoribonucleases are enzymes that cleave RNA molecules by removing terminal nucleotides from the 3′ or 5′ end of the RNA molecules. They are key factors in RNA metabolism and have a relevant role in the processing and degradation of all types of RNAs. The 3′ to 5′ exoribonucleases are divided into families, according to their sequence and structural characteristics. The PDX family contains phosphate-dependent degradative enzymes, which can also perform the synthesis of RNA tails when phosphate is limiting. The RNB family contains hydrolytic enzymes with a similar domain organization. All proteins from this widespread family present the characteristic RNB domain responsible for the 3′ to 5′ exoribonuclease activity. In eukaryotes they can act alone or in a complex, the exosome, where they are the only active component. Finally, the DEDD family includes both RNA and DNA exonucleases and they present a similar mechanism of action. In this chapter, we will summarize the available information regarding the 3′ to 5′ exoribonucleases and discuss their importance for the RNA metabolism.
Original languageUnknown
Title of host publicationRibonucleases
EditorsA. W. Nicholson
Place of PublicationHeidelberg
PublisherSpringer Berlin
Pages193-222
ISBN (Print)978-3-642-21078-5
Publication statusPublished - 1 Jan 2011

Publication series

NameNucleic Acids and Molecular Biology
PublisherSpringer Berlin
Number26

Cite this

Matos, R. G., Pobre, V., Reis, F., Malecki, M. G., Andrade, J. E., & Arraiano, C. M. (2011). Structure and degradation mechanisms of 3′ to 5′ exoribonucleases. In A. W. Nicholson (Ed.), Ribonucleases (pp. 193-222). (Nucleic Acids and Molecular Biology; No. 26). Heidelberg: Springer Berlin.
Matos, R.G. ; Pobre, V. ; Reis, Filipa ; Malecki, Michal Grzegorz ; Andrade, Jose Eduardo ; Arraiano, Cecilia Maria. / Structure and degradation mechanisms of 3′ to 5′ exoribonucleases. Ribonucleases. editor / A. W. Nicholson. Heidelberg : Springer Berlin, 2011. pp. 193-222 (Nucleic Acids and Molecular Biology; 26).
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Matos, RG, Pobre, V, Reis, F, Malecki, MG, Andrade, JE & Arraiano, CM 2011, Structure and degradation mechanisms of 3′ to 5′ exoribonucleases. in AW Nicholson (ed.), Ribonucleases. Nucleic Acids and Molecular Biology, no. 26, Springer Berlin, Heidelberg, pp. 193-222.

Structure and degradation mechanisms of 3′ to 5′ exoribonucleases. / Matos, R.G.; Pobre, V.; Reis, Filipa; Malecki, Michal Grzegorz; Andrade, Jose Eduardo; Arraiano, Cecilia Maria.

Ribonucleases. ed. / A. W. Nicholson. Heidelberg : Springer Berlin, 2011. p. 193-222 (Nucleic Acids and Molecular Biology; No. 26).

Research output: Chapter in Book/Report/Conference proceedingChapter

TY - CHAP

T1 - Structure and degradation mechanisms of 3′ to 5′ exoribonucleases

AU - Matos, R.G.

AU - Pobre, V.

AU - Reis, Filipa

AU - Malecki, Michal Grzegorz

AU - Andrade, Jose Eduardo

AU - Arraiano, Cecilia Maria

PY - 2011/1/1

Y1 - 2011/1/1

N2 - Exoribonucleases are enzymes that cleave RNA molecules by removing terminal nucleotides from the 3′ or 5′ end of the RNA molecules. They are key factors in RNA metabolism and have a relevant role in the processing and degradation of all types of RNAs. The 3′ to 5′ exoribonucleases are divided into families, according to their sequence and structural characteristics. The PDX family contains phosphate-dependent degradative enzymes, which can also perform the synthesis of RNA tails when phosphate is limiting. The RNB family contains hydrolytic enzymes with a similar domain organization. All proteins from this widespread family present the characteristic RNB domain responsible for the 3′ to 5′ exoribonuclease activity. In eukaryotes they can act alone or in a complex, the exosome, where they are the only active component. Finally, the DEDD family includes both RNA and DNA exonucleases and they present a similar mechanism of action. In this chapter, we will summarize the available information regarding the 3′ to 5′ exoribonucleases and discuss their importance for the RNA metabolism.

AB - Exoribonucleases are enzymes that cleave RNA molecules by removing terminal nucleotides from the 3′ or 5′ end of the RNA molecules. They are key factors in RNA metabolism and have a relevant role in the processing and degradation of all types of RNAs. The 3′ to 5′ exoribonucleases are divided into families, according to their sequence and structural characteristics. The PDX family contains phosphate-dependent degradative enzymes, which can also perform the synthesis of RNA tails when phosphate is limiting. The RNB family contains hydrolytic enzymes with a similar domain organization. All proteins from this widespread family present the characteristic RNB domain responsible for the 3′ to 5′ exoribonuclease activity. In eukaryotes they can act alone or in a complex, the exosome, where they are the only active component. Finally, the DEDD family includes both RNA and DNA exonucleases and they present a similar mechanism of action. In this chapter, we will summarize the available information regarding the 3′ to 5′ exoribonucleases and discuss their importance for the RNA metabolism.

M3 - Chapter

SN - 978-3-642-21078-5

T3 - Nucleic Acids and Molecular Biology

SP - 193

EP - 222

BT - Ribonucleases

A2 - Nicholson, A. W.

PB - Springer Berlin

CY - Heidelberg

ER -

Matos RG, Pobre V, Reis F, Malecki MG, Andrade JE, Arraiano CM. Structure and degradation mechanisms of 3′ to 5′ exoribonucleases. In Nicholson AW, editor, Ribonucleases. Heidelberg: Springer Berlin. 2011. p. 193-222. (Nucleic Acids and Molecular Biology; 26).