The KH domain occurs in a diverse set of RNA‐binding proteins that include the antiterminator NusA and is probably involved in binding to nucleic acid

Gibson, Toby J.; Thompson, Julie; Heringa, Jaap

doi:10.1016/0014-5793(93)80152-k

Cited by 192 publications

(155 citation statements)

References 39 publications

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“…If it is truncated by five amino acids at either end, the binding is reduced (It0 et al, 1994;this paper). Most previous descriptions of KH domains (Dreyfuss et al, 1993;Siomi et al, 1993a;Gibson et al, 1993;Buckanovich et al, 1993;Siomi et al, 1994Siomi et al, , 1995Duncan et al, 1994) have only included the N-terminal part, ending shortly after the middle variable region, and this is clearly insufficient for nucleic Fig. 5.…”

Section: Discussionmentioning

confidence: 99%

“…Recently, a novel motif was detected in heterogenous nuclear ribonucleoprotein K (hnRNP-K) (Matunis et al, 1992; and one or more were soon discovered in a number of other putative nucleic acid binding proteins from both eukaryotes, eubacteria and archaea (Gibson et al, 1993;Siomi et al, 1993a;. These include the fragile-X protein (FMR1) (Verkerk et al, 1991;Siomi et al, 1993b), the Ri auto antigen (nova) (Buckanovich et al, 1993), a putative transcription activator FBP (Duncan et al, 1994), the poly(rC)-binding proteins (PCBP) 1 and 2 (Leffers et al, 1995) and HBP (McKnight et al, 1992) from human, the yeast merl (Engebrecht and Roeder, 1990) and HX proteins (Delahodde et al, 1986), ribosomal proteins from different species (Kao et al, 1990;Klenk et al, 1991) and the bacterial nusA (see Musco et al, 1996, for latest review).…”

Section: Hagen Denmarkmentioning

confidence: 99%

“…These include the fragile-X protein (FMR1) (Verkerk et al, 1991;Siomi et al, 1993b), the Ri auto antigen (nova) (Buckanovich et al, 1993), a putative transcription activator FBP (Duncan et al, 1994), the poly(rC)-binding proteins (PCBP) 1 and 2 (Leffers et al, 1995) and HBP (McKnight et al, 1992) from human, the yeast merl (Engebrecht and Roeder, 1990) and HX proteins (Delahodde et al, 1986), ribosomal proteins from different species (Kao et al, 1990;Klenk et al, 1991) and the bacterial nusA (see Musco et al, 1996, for latest review). A 45-55-amino-acid motif was named KH for K-homologous, with reference to the initial identification of the motif in hnRNP-K (Siomi et al, 1993a;Gibson et al, 1993). Based on our observations of hnRNP-K and the repeated sequences found in HBP (McKnight et al, 1992), we later extended this to cover 65-70 amino acids .…”

Section: Hagen Denmarkmentioning

confidence: 99%

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Characterisation of the Nucleic‐Acid‐Binding Activity of KH Domains Different Properties of Different Domains

Dejgaard

Leffers

1996

European Journal of Biochemistry

118

114

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The KH module is a sequence motif recently identified in a number of diversified RNA-binding proteins and suggested to be the functional element responsible for RNA binding. So far, however, this hypothesis has not received direct experimental support. We have expressed the three KH-domains from heterogeneous nuclear ribonucleoprotein K (hnRNP-K), the poly(C)-binding proteins PCBP-1 and PCBP-2, the first three to four domains from the high-density binding protein HBP, the one and a half domain from the archaeon Halobacterium halobium ORF139 and one and a half domain of the fragile-X protein FMRl in Escherichia coli and analysed their nucleic-acid-binding properties in vitro. The results showed that the in vitro poly(rC)-binding activity of hnRNP-K can be assigned to KH-domain 3, whereas both domains 1 and 3 in the PCBPs bind poly(rC). In addition, all these domains exhibit binding activity towards other nucleic acids, albeit at a significantly lower level. The first KH domain from the FMRl protein binds poly(rG) and single-stranded and double-stranded DNA. The N-terminal three or four domains from HBP bind poly(rG) and, at a much lower level, single-stranded and double-stranded DNA. Thus, single KH domains are discrete and independent nucleic-acid-binding units. Moreover, different KH domains bind different nucleic acids, suggesting that KH domains are composed of a conserved, weakly nucleic-acid-binding, structure that is fine tuned, by sequence variation, resulting in sequencespecific nucleic-acid-binding entities.

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Section: Discussionmentioning

confidence: 99%

Section: Hagen Denmarkmentioning

confidence: 99%

Section: Hagen Denmarkmentioning

confidence: 99%

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Characterisation of the Nucleic‐Acid‐Binding Activity of KH Domains Different Properties of Different Domains

Dejgaard

Leffers

1996

European Journal of Biochemistry

118

114

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“…Sam68 is a nuclear protein that consists of at least six proline rich regions, an RNA binding region referred to as the hnRNP K homology (KH) domain (Gibson et al, 1993;Siomi et al, 1993) and a tyrosinerich C-terminal region (Wong et al, 1992;Fumagalli et al, 1994;Chen et al, 1997;Ishidate et al, 1997). Sam68 binds to poly(U) homopolymeric ribonucleotides, in vitro (Taylor and Shalloway, 1994;, and its ability to bind ribonucleotides can be negatively regulated by tyrosine phosphorylation, as well as by interactions with the Src SH3 domain (Taylor et al, 1995;Wang et al, 1995).…”

Section: Nuclear and Perinuclear Targets Of Srcmentioning

confidence: 99%

Selected glimpses into the activation and function of Src kinase

2000

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Since the discovery of the v-src and c-src genes and their products, much progress has been made in the elucidation of the structure, regulation, localization, and function of the Src protein. Src is a non-receptor protein tyrosine kinase that transduces signals that are involved in the control of a variety of cellular processes such as proliferation, di erentiation, motility, and adhesion. Src is normally maintained in an inactive state, but can be activated transiently during cellular events such as mitosis, or constitutively by abnormal events such as mutation (i.e. v-Src and some human cancers). Activation of Src occurs as a result of disruption of the negative regulatory processes that normally suppress Src activity, and understanding the various mechanisms behind Src activation has been a target of intense study. Src associates with cellular membranes, in particular the plasma membrane, and endosomal membranes. Studies indicate that the di erent subcellular localizations of Src could be important for the regulation of speci®c cellular processes such as mitogenesis, cytoskeletal organization, and/or membrane tra cking. This review will discuss the history behind the discovery and initial characterization of Src and the regulatory mechanisms of Src activation, in particular, regulation by modi®cation of the carboxyterminal regulatory tyrosine by phosphatases and kinases. Its focus will then turn to the di erent subcellular localizations of Src and the possible roles of nuclear and perinuclear targets of Src. Finally, a brief section will review some of our present knowledge regarding Src involvement in human cancers. Oncogene (2000) 19, 5620 ± 5635.

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“…Several laboratories showed that a subfamily of hnRNPs, hnRNP K and hnRNP E1/E2, functions in translational regulation and/or mRNA stabilization in haematopoiesis. These proteins all bear three copies of an RNA binding motif, the hnRNP K homology (KH)-domain (Siomi et al, 1993, Gibson et al, 1993 consisting of 65-70 amino acids (Dejgaard andLeffers, 1996, Musco et al, 1996). In contrast to hnRNP E1/E2, hnRNP K carries additional domains: An N-terminal bipartite nuclearlocalization signal (NLS) and an hnRNP K-specific nuclear shuttling signal located between the second and third KHdomain, which confers the capacity for bi-directional transport across the nuclear envelope (Matunis et al, 1992, Michael et al, 1995.…”

Section: Introductionmentioning

confidence: 99%

Control of mRNA translation and stability in haematopoietic cells: The function of hnRNPs K and E1/E2

Ostareck-Lederer

Ostareck

2004

Biology of the Cell

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Studies on the post-transcriptional regulation of gene expression in haematopoietic cells have uncovered that a subfamily of heterogeneous nuclear ribonucleoproteins (hnRNPs) is involved in cytoplasmic gene regulation. HnRNP K and hnRNP E1/E2 share a common structural motif, the hnRNP K homology (KH) domain, which provides a structural basis for mRNA binding. The KH-domains are components of a modular system, which enables these proteins to engage in both, protein/nucleic acid and protein/protein interactions, the latter generating connectivity to cell signalling events. As components of different mRNA-protein complexes, hnRNP K and hnRNP E1/E2 function in the control of mRNA translation and mRNA stability in haematopoietic cell differentiation.

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The KH domain occurs in a diverse set of RNA‐binding proteins that include the antiterminator NusA and is probably involved in binding to nucleic acid

Cited by 192 publications

References 39 publications

Characterisation of the Nucleic‐Acid‐Binding Activity of KH Domains Different Properties of Different Domains

Characterisation of the Nucleic‐Acid‐Binding Activity of KH Domains Different Properties of Different Domains

Selected glimpses into the activation and function of Src kinase

Control of mRNA translation and stability in haematopoietic cells: The function of hnRNPs K and E1/E2

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